{"title":"MYC Protein: Target Overview, Research Applications, and Selection Guide","description":"","products":[{"product_id":"biotinylated-recombinant-human-myc-proto-oncogene-protein-myc-protein-mbp-his-avi-blc-01093p","title":"Biotinylated Recombinant Human Myc Proto-Oncogene Protein (MYC) Protein (MBP\u0026His-Avi)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiotinylated Recombinant Human Myc Proto-Oncogene Protein (MYC) Protein (MBP\u0026amp;His-Avi) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P01106          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e(Class E basic helix-loop-helix protein 39)(bHLHe39)(Proto-oncogene c-Myc)(Transcription factor p64)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-MBP\u0026amp;C-6His-Avi\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-439aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e96.6 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTranscription\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTranscription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus, nucleoplasm. Nucleus, nucleolus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7553           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            113970           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4609           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000367207           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30226609            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            lncRNA THOR is up-regulated in retinoblastoma, and its over-expression significantly enhances the malignant phenotype transformation of retinoblastoma cells by up-regulating c-myc and TGF2BP1 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30119193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we demonstrate that neither MYC IHC nor MYC FISH alone is a sufficient screening mechanism for identification of the clinically relevant entities of HGBLwR or DEL            \u003ca rel=\"nofollow\"\u003e             PMID:                        28868942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Because RPL23 is encoded by a target gene of c-Myc, the RPL23\/Miz-1\/c-Myc regulatory circuit provides a feedback loop that links efficient RPL23 expression with c-Myc's function to suppress Miz-1-induced Cdk inhibitors and thereby leads to apoptotic resistance in higher-risk myelodysplastic syndrome patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28539603            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GATAD2B interacts with C-MYC to enhance KRAS driven tumor growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30013058            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            low expression of c-Myc protein predicts poor outcomes in patients with HCC with hepatectomy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29690860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Combined, these findings suggest that c-Myc could transcriptionally regulate TCRP1 in cell lines and clinical samples and identified the c-Myc-TCRP1 axis as a negative biomarker of prognosis in tongue and lung cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28623290            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Kazakh and Han patients with esophageal squamous cell carcinoma with Glut1 c-myc co-expression had poorer prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29629851            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC activation in papillary clear cell renal cell carcinoma leads to a worse prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28593993            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            could not find any relationship between Bcl-2, c-Myc and EBER-ISH positivity and the low\/high IPS groups in classical Hodgkin lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29708579            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fluorescence in situ hybridization studies (histologic sections) confirmed translocations of MYC (8q24), BCL2 (18q21) and BCL6 (3q27) in all patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30043475            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            topical mevastatin accelerates wound closure by promoting epithelialization via multiple mechanisms: modulation of GR ligands and induction of the long noncoding RNA Gas5, leading to c-Myc inhibition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CCND1 , C-MYC , and FGFR1 amplifications were observed in 34.28%, 28.57%, and 17.14% of the 35 samples (invasive ductal breast carcinoma).            \u003ca rel=\"nofollow\"\u003e             PMID:                        30119151            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that MYC induction of REV-ERBalpha is both persistent and recurrent across many inducible MYC model systems.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28332504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HUWE1 overexpression could functionally suppress prostate carcinoma development both in vitro and in vivo, possibly by inverse regulation of c-Myc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29966975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Menin functions as an oncogenic regulatory factor that is critical for MYC-mediated gene transcription.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28474697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Melatonin disturbs SUMOylation-mediated crosstalk between c-Myc and nestin via MT1 activation and promotes the sensitivity of paclitaxel in brain cancer stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29654697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FBP1 modulates the sensitivity of pancreatic cancer cells to BET inhibitors by decreasing the expression of c-Myc. These findings highlight FBP1 could be used as a therapeutic niche for patient-tailored therapies            \u003ca rel=\"nofollow\"\u003e             PMID:                        30201002            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR135a directly bound to UCA1 and the 3' untranslated region of cmyc, and UCA1 competed with cmyc for miR135a binding.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC directly regulates DANCR and plays important role in cancer cell proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29180471            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this review, we provide support to the hypothesis that the cooperation of c-Myc with transcriptional cofactors mediates c-Myc-induced cellular functions. We produce evidence that recently identified cofactors are involved in c-Myc control of survival mechanisms of cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        30261904            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            4-chlorobenzoyl berbamine (CBBM) inhibits the JAK2\/STAT3 pathway, leading to reduced c-Myc transcription. Collectively, these findings suggest that CBBM could be a promising lead compound for treatment of c-Myc-driven diffuse large B cell lymphoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30099568            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results revealed that C-MYC protein is highly expressed in colon cancer tissues, mainly in the cell nucleus and was identified as a direct target for mir-184. C-MYC appeared to participate in cell cycle regulation and malignant transformation to colon cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28782841            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MACC1 and c-Myc are highly expressed in serum and tumor tissues of EC patients. Both are correlated with TNM stage, primary infiltration, and lymph node or distal metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29984790            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study provides an interesting example using chemical biological approaches for determining distinct biological consequences from inhibiting vs. activating an E3 ubiquitin ligase and suggests a potential broad therapeutic strategy for targeting c-MYC in cancer treatment by pharmacologically modulating cIAP1 E3 ligase activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30181285            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The data demonstrated that 10058F4, a cMyc inhibitor, increased the growth inhibition, G0\/G1 phase arrest and apoptosis of the NALM6 and CEM cells as induced by dexamethasone (DXM), a type of GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749488            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-MYC\/BCL2 protein co-expression is associated with non-germinal center B-cell in Diffuse Large B-Cell Lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29801406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-Myc was capable of upregulating HP1gamma by directly binding to the E-box element in the first intron of HP1gamma gene, and the upregulated HP1gamma, in turn, repressed the expression of miR-451a by enhancing H3K9 methylation at the promoter region of miR-451a.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28967902            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A subset of pancreatic acinar cell carcinomas shows c-MYC alterations including gene amplification and chromosome 8 polysomy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29721608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression and Clinical Significance of LC-3 and P62 in Non-small Cell Lung Cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29945702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of the current study demonstrate presence of the IDH1 R132H mutation in primary human glioblastoma cell lines with upregulated HIF-1alpha expression, downregulating c-MYC activity and resulting in a consequential decrease in miR-20a, which is responsible for cell proliferation and resistance to standard temozolomide treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29625108            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a novel signal circuit of Stat3\/Oct-4\/c-Myc was identified for regulating stemness-mediated Doxorubicin resistance in triple-negative breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29750424            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC amplification and MYC overexpression occurred almost exclusively in secondary cutaneous angiosarcoma in our series.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29135507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with the development of prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29554906            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circular RNA hsa_circRNA_103809 promotes lung cancer progression via facilitating ZNF121-dependent MYC expression by sequestering miR-4302.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29698681            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors conclude that quantitative measurements of intratumor heterogeneity by multiplex FISH, detection of MYC amplification and TP53 mutation could augment prognostication in breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29181861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCYT1A was upregulated by MYC, which resulted in the induction of aberrant choline metabolism and the inhibition of B-lymphoma cell necroptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28686226            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cryptic t(3;8)(q27;q24) and\/or MYC-BCL6 linkage associated with MYC expression by immunohistochemistry is frequent in multiple-hit B-cell lymphomas.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28665415            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD30+ diffuse large B-cell lymphoma has characteristic clinicopathological features mutually exclusive with MYC gene rearrangement and negatively associated with BCL2 protein expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29666157            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High MYC amplification is associated with HER2 positive breast cancers in African American women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29523126            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest that MYC acts as a master coordinator that inversely modulates the impact of cell cycle and circadian clock on gene expression via its interaction with MIZ1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27339797            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In our study, the c-myc oncogene was amplified in 11.1% of BPH samples. Bivariate analysis failed to reveal any significant association between oncogene amplification and the clinicopathologic variables examined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29234244            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic variation at the 8q24.21 renal cancer susceptibility locus affects HIF1A and HIF1B binding to a MYC enhancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27774982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that miR-34a enhanced the sensitivity to cisplatin by upregulation of c-Myc and Bim pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29060932            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Luciferase reporter assay showed that c-Myc, an oncogene that regulating cell survival, angiogenesis and metastasis, was a direct target of miR-376a. Over-expression of miR-376a decreased the mRNA and protein levels of c-Myc in A549 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28741879            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present findings show that expression of c-MYC has prognostic value in squamous cell carcinoma of the tongue, and could be useful in choice of therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28393404            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Multivariable analysis indicated that IPI (P = 0.002), chemotherapy regimens (P = 0.017), and MYC gene rearrangements (P = 0.004) were independent adverse prognostic factors for all diffuse large B cell Lymphoma(DLBCL) patients in this study. Results demonstrated that the poor survival of DLBCL patients with HBV infection was closely involved in chemotherapy regimens, IPI, and MYC gene rearrangements            \u003ca rel=\"nofollow\"\u003e             PMID:                        29209623            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC extra copy in diffuse large B-cell lymphoma is an independent poor prognostic factor            \u003ca rel=\"nofollow\"\u003e             PMID:                        28776574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The c-Myc\/miR-200b\/PRDX2 loop regulates colorectal cancer (CRC) progression and its disruption enhances tumor metastasis and chemotherapeutic resistance in CRC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29258530            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998463230177,"sku":"BLC-01093P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP015270HU-B-SDS.jpg?v=1690497265"},{"product_id":"recombinant-human-2-5a-dependent-ribonuclease-rnasel-protein-myc-blc-01950p","title":"Recombinant Human 2-5A-Dependent Ribonuclease (RNASEL) Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human 2-5A-Dependent Ribonuclease (RNASEL) Protein (Myc) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           Q05823          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRNASEL\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRibonuclease 4 (Ribonuclease L) (RNase L)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eC-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKKNGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGHVEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTDSDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGKLKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRGEDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFEDLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFDKWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTHSPNKPQCDGAGGASGLASPGC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-741aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e85.1 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOthers\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEndoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover. Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCytoplasm. Mitochondrion.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eProtein kinase superfamily\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            10050           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            176807           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:6041           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000356530           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28418037            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Our study suggests that RNASEL:p.Glu265* may be a genetic modifier of risk for early-onset breast cancer predisposition in carriers of high-risk mutations.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29422015            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results reported in the present study suggest a sex-specific interaction between miR-146a and RNASEL genes in melanoma skin cancer susceptibility.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28654546            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrate that ablation of RNase L activity promotes survival of ADAR1 deficient cells even in the presence of MDA5 and MAVS, suggesting that the RNase L system is the primary sensor pathway for endogenous dsRNA that leads to cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28362255            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mutations in the genes glucokinase regulatory protein (GCKR), RNase L (RNASEL), leukocyte immunoglobulin-like receptor 3 (LILRA3), and dynein axonemal heavy chain 10 (DNAH10) segregated with elevated HDLc levels in families, while no mutations associated with low HDLc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24891332            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggest that beside the RLR pathway, RNase L cleavage products can also activate the NLRP3-inflammasome pathway, which requires DHX33 (DExD\/H-box helicase) and the mitochondrial adaptor protein MAVS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26987611            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study provides the evidence that germline variations in RNASEL are associated with fatal PCa in men (Gleason score \u0026gt;7 for rs486907 and RNASEL underexpressed [P = 0.007] in patients with PCa).            \u003ca rel=\"nofollow\"\u003e             PMID:                        27318894            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            By sequencing abundant RNA fragments generated by RNase L in cell lines, we identify site-specific cleavage of two groups of noncoding RNAs: Y-RNAs, whose function is poorly understood, and cytosolic tRNAs, which are essential for translation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28808124            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RNASEL rs3738579 genotype was significantly related to severe necroinflammatory activity (NIA) grade of chronic hepatitis C patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28704535            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum RNase-L levels were inversely associated with metabolic syndrome and age.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28399925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We show that mutations in RNase L found in HPC patients may promote prostate cancer by increasing expression of AR-responsive genes and cell motility and identify novel roles of RNase L as a prostate cancer susceptibility gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28257035            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suggest that naturally occurring mutations in the RNase L gene might promote enhanced prostate cancer cell migration and metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26517238            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review outlines the role of RNase-L in antimicrobial immunity and the cytoskeleton-associated innate response. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        26760998            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that RNA decay by ribonuclease L (RNase L) has an important role in homeostasis and serves as a suppressor of cell adhesion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26668391            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Single Nucleotide Polymorphisms in RNASEL involved in the immune response are generally not associated with intraprostatic inflammation in men without a Prostate cancer diagnosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26771888            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OAS3 displayed a higher affinity for dsRNA in intact cells than either OAS1 or OAS2, consistent with its dominant role in RNase L activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26858407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Tanslation of vaccinia virus A27L and B5R genes is independent of PKR activation, but their expression is dependent on the RNase L activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26656695            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results demonstrate a novel role of RNase L generated small RNAs in cross-talk between autophagy and apoptosis that impacts the fate of cells during viral infections and cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26263979            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Among 794 RNASEL Ssingle nucleotide polymorphism (SNPs) entries 124 SNPs were found nonsynonymous (ns) from which SIFT predicted 13 nsSNPs as nontolerable whereas PolyPhen-2 predicted 28.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26236721            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Virus infection and RNase L activation disrupt its association with Filamin A and release RNase L to mediate its canonical nuclease-dependent antiviral activities.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25352621            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data show that RNase L targets specific sites in both host and viral RNAs to restrict influenza virus replication when NS1 protein is disabled.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25540362            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The IFNs inhibit viral infections in part through the 2',5'-oligoadenylate (2-5A) synthetase (OAS)\/RNase L pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24905202            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a model of feedback regulation in which RNase L and TTP target SRF mRNA and SRF-induced transcripts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25301952            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data suggest that RNASEL, an enzyme involved in RNA turnover, is controlled by miR-146a and may be important in NMSC etiology            \u003ca rel=\"nofollow\"\u003e             PMID:                        24699816            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The combined high affinity for double-stranded RNA and the capability to produce 2'-5'-linked oligoadenylates of sufficient length to activate RNase L suggests that OAS3 is a potent activator of RNase L.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25275129            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study identified three RNASEL variants that are associated with risk for prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21360564            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RNAse L gene SNP 1385G\u0026gt;A does not have a clear clinical significance in CHC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25286525            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RNase L activity limits FFA\/obesity-induced impairment of insulin response in muscle cells via TLR3 and MnSOD expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24651439            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This work identifies novel roles for IFN-beta and RNase L in cell barrier functions that are targeted by bacterial effectors to escape host defense mechanisms and promote virulence.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24733098            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Association between SNPs from RNASEL and chromosome 8q24 with the risk of prostate cancer, and its aggressiveness, in a Hispanic (Chilean) population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24224612            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study reports 2.8 and 2.1 angstrom crystal structures of human RNase L in complexes with synthetic and natural ligands and a fragment of an RNA substrate.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24578532            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We show an association between RNASEL SNP rs12757998 and outcome after radiation therapy for prostate cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        23382116            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the structural changes of human RNase L as a result of interactions with four different activators: natural 2-5 pA(4) and three tetramers with 3'-end AMP            \u003ca rel=\"nofollow\"\u003e             PMID:                        22691533            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that miR-29 acts via 4 target sites within the RNASEL 3' UTR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23113544            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RNASEL mutations are associated with xenotropic murine leukemia virus and its R426Q polymorphism in patients with prostate cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        23098452            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Two molecules of 2-5A at a time tether RNase L monomers via the ankyrin-repeat (ANK) domain. Each ANK domain harbors two distinct sites for 2-5A recognition that reside 50 A apart.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23084743            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            among the members of the OAS family, OAS1 p46 and OAS3 p100 mediate the RNase L-dependent antiviral activity against HCV            \u003ca rel=\"nofollow\"\u003e             PMID:                        23196181            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RNase L induces autophagy via c-Jun N-terminal kinase and double-stranded RNA-dependent protein kinase signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23109342            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study found that RNase L is highly expressed in lung cancer cells with significantly decreased enzymatic activity due to an increase of RLI, a specific inhibitor of RNase L            \u003ca rel=\"nofollow\"\u003e             PMID:                        22925698            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Positive selection has operated on the RNASEL gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22513284            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Statistically significant differences were found between controls and patients in some of the genotyped regions of the RNASEL gene            \u003ca rel=\"nofollow\"\u003e             PMID:                        22464196            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            genotypes associated with the worst prognoses in prostate cancer are G\/G in D541E, A\/A in R462Q and A\/G in I97L.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22083266            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The RNASEL 541Gln allele might be a low-penetrent risk factor for sporadic prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21656378            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Five SNPs were validated as being significantly associated with prostate cancer mortality, one each in the LEPR, CRY1, RNASEL, IL4, and ARVCF genes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21846818            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The RNASEL -1385G\/A polymorphism is associated with cancer risk in African descendents.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21221811            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ribonuclease L (RNASEL) protein was shown to be up-regulated in lopinavir-treated SiHa cells, which was confirmed by PCR and western blot. Targeted silencing of RNASEL reduced the sensitivity of SiHa cells to lopinavir.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21685539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Codon 462 polymorphisms within the RNASEL gene are not associated with an increased risk of cervical cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21665181            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the IQ motif-containing Ras GTPase-activating-like protein 1 (IQGAP1) can associate with RNase L, and that phosphorylation occurs on the IQGAP1, and works as a regulator in apoptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20875083            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic variation is associated with RNASEL associated with prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20576793            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies suggest that the expression of Xpr1 and certain genotypes of the RNASEL gene, which could restrict XMRV infection, may play important roles in defining XMRV tropisms in certain cell types.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20410264            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998553473249,"sku":"BLC-01950P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP313223HU-SDS.jpg?v=1690500071"},{"product_id":"recombinant-human-bone-morphogenetic-protein-3-bmp3-protein-myc-blc-02080p","title":"Recombinant Human Bone Morphogenetic Protein 3 (BMP3) Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Bone Morphogenetic Protein 3 (BMP3) Protein (Myc) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P12645          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBMP3\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBMP-3; BMP-3A; bmp3; BMP3_HUMAN; BMP3A; Bone morphogenetic protein 3 (osteogenic); Bone morphogenetic protein 3; Bone morphogenetic protein 3A; Osteogenin\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eC-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQWIEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGACQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFFDENKNVVLKVYPNMTVESCACR\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e363-472aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length of Mature Protein\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.9 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eDevelopmental Biology\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth factor of the TGF-beta superfamily that plays an essential role in developmental process by inducing and patterning early skeletal formation and by negatively regulating bone density. Antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentitation and ossification. Initiates signaling cascades by associating with type II receptor ACVR2B to activate SMAD2-dependent and SMAD-independent signaling cascades including TAK1 and JNK pathways.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            1070           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            112263           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:651           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000282701           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29892846            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            BMP3 - the biomarker of a currently in-use multi-target stool DNA test was commonly expressed in tumor tissue specimens, independent of Fecal Immunochemical Test result.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28044229            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Methylation level in stool decreases dramatically following colorectal cancer resection            \u003ca rel=\"nofollow\"\u003e             PMID:                        24993691            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Bone morphogenic protein 3 signaling in the regulation of osteogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23127436            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            As an addition to PRKG2 and RASGEFIB genes, we propose to include BMP3 gene as the principal determinant of the observed common phenotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22303795            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a critical link between HNF1A-MODY-induced alterations in Bmp-3 expression and insulin gene levels            \u003ca rel=\"nofollow\"\u003e             PMID:                        21628466            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Features supportive of positive selection in the BMP3 gene were found including the presence of an excess of nonsynonymous mutations in modern humans, and a significantly lower genetic diversity that deviates from neutrality            \u003ca rel=\"nofollow\"\u003e             PMID:                        20532035            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that promotor region methylation of the BMP3 gene may cause gastric carcinoma in Chinese people.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20238409            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrate that BMP-3 stimulates mesenchymal stem cell proliferation via the TGF-beta\/activin signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20143330            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression signals of BMP3 mRNA in malignant schwannoma were relatively lower than in benign lesions            \u003ca rel=\"nofollow\"\u003e             PMID:                        11642720            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP-3 receptor specificity is controlled by the interaction of Lys-30 of BMP-3 with Glu-76 of ActRIIb            \u003ca rel=\"nofollow\"\u003e             PMID:                        17924656            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP3 silencing is an early and frequent event in colorectal tumors progressing via the serrated and traditional pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18311777            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998565957857,"sku":"BLC-02080P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP002739HUf1-SDS.jpg?v=1690500497"},{"product_id":"recombinant-crassostrea-gigas-a-kinase-anchor-protein-7-isoform-x2-protein-myc-blc-02085p","title":"Recombinant Crassostrea Gigas A-Kinase Anchor Protein 7 Isoform X2 Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Crassostrea Gigas A-Kinase Anchor Protein 7 Isoform X2 Protein (Myc) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           XP_011412823.1          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eXP_011412823.1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCrassostrea gigas\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eC-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMARRKRESPNYFLAIQITEDEIKRNVREIQEIILAKEENLSTAMIGIDTLHLTLGVYYLEDGFSIIQIKRALDKFHSQLKAADFVPPCLKVSTLGHFNHKVLYASLEENQGLEELNTLVNGVRTSLENDGVFTADDRYTPHVTISKMSKDMNRLRKLGVSRIDPSHYQEKRTAYFGQQVVKSIQLCAMNVPKTESGYYYVEHEIMFS\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-207aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25.8 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOthers\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998566613217,"sku":"BLC-02085P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP2586DXQ_M_f1-SDS.jpg?v=1690561124"},{"product_id":"recombinant-human-myc-proto-oncogene-protein-myc-protein-his-blc-02815p","title":"Recombinant Human Myc Proto-Oncogene Protein (MYC) Protein (His)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Myc Proto-Oncogene Protein (MYC) Protein (His) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 90% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P01106          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAU016757; Avian myelocytomatosis viral oncogene homolog; bHLHe39; c Myc; Cellular myelocytomatosis oncogene; Class E basic helix-loop-helix protein 39; MGC105490; MRTL; Myc; Myc protein; Myc proto oncogene protein; Myc proto-oncogene protein; myc-related translation\/localization regulatory factor; MYC_HUMAN; Myc2; myca; MYCC; Myelocytomatosis oncogene a; Myelocytomatosis oncogene; Niard; Nird; oncogene c-Myc; Oncogene Myc; OTTHUMP00000158589; OTTHUMP00000227763; Proto-oncogene c-Myc; Protooncogene homologous to myelocytomatosis virus; RNCMYC; Transcription factor p64; Transcriptional regulator Myc-A; V-Myc avian myelocytomatosis viral oncogene homolog; v-myc myelocytomatosis viral oncogene homolog (avian); zc-myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-6His\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPNPARGHSV CSTSSLYLQD LSAAASECID PSVVFPYPLN DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENVKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAEE QKLISEEDLL RKRREQLKHK LEQLRNSCA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-439\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull length protein\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e52.8 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTranscription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus, nucleoplasm. Nucleus, nucleolus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7553           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            113970           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4609           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000367207           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30226609            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            lncRNA THOR is up-regulated in retinoblastoma, and its over-expression significantly enhances the malignant phenotype transformation of retinoblastoma cells by up-regulating c-myc and TGF2BP1 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30119193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we demonstrate that neither MYC IHC nor MYC FISH alone is a sufficient screening mechanism for identification of the clinically relevant entities of HGBLwR or DEL            \u003ca rel=\"nofollow\"\u003e             PMID:                        28868942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Because RPL23 is encoded by a target gene of c-Myc, the RPL23\/Miz-1\/c-Myc regulatory circuit provides a feedback loop that links efficient RPL23 expression with c-Myc's function to suppress Miz-1-induced Cdk inhibitors and thereby leads to apoptotic resistance in higher-risk myelodysplastic syndrome patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28539603            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GATAD2B interacts with C-MYC to enhance KRAS driven tumor growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30013058            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            low expression of c-Myc protein predicts poor outcomes in patients with HCC with hepatectomy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29690860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Combined, these findings suggest that c-Myc could transcriptionally regulate TCRP1 in cell lines and clinical samples and identified the c-Myc-TCRP1 axis as a negative biomarker of prognosis in tongue and lung cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28623290            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Kazakh and Han patients with esophageal squamous cell carcinoma with Glut1 c-myc co-expression had poorer prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29629851            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC activation in papillary clear cell renal cell carcinoma leads to a worse prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28593993            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            could not find any relationship between Bcl-2, c-Myc and EBER-ISH positivity and the low\/high IPS groups in classical Hodgkin lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29708579            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fluorescence in situ hybridization studies (histologic sections) confirmed translocations of MYC (8q24), BCL2 (18q21) and BCL6 (3q27) in all patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30043475            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            topical mevastatin accelerates wound closure by promoting epithelialization via multiple mechanisms: modulation of GR ligands and induction of the long noncoding RNA Gas5, leading to c-Myc inhibition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CCND1 , C-MYC , and FGFR1 amplifications were observed in 34.28%, 28.57%, and 17.14% of the 35 samples (invasive ductal breast carcinoma).            \u003ca rel=\"nofollow\"\u003e             PMID:                        30119151            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that MYC induction of REV-ERBalpha is both persistent and recurrent across many inducible MYC model systems.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28332504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HUWE1 overexpression could functionally suppress prostate carcinoma development both in vitro and in vivo, possibly by inverse regulation of c-Myc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29966975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Menin functions as an oncogenic regulatory factor that is critical for MYC-mediated gene transcription.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28474697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Melatonin disturbs SUMOylation-mediated crosstalk between c-Myc and nestin via MT1 activation and promotes the sensitivity of paclitaxel in brain cancer stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29654697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FBP1 modulates the sensitivity of pancreatic cancer cells to BET inhibitors by decreasing the expression of c-Myc. These findings highlight FBP1 could be used as a therapeutic niche for patient-tailored therapies            \u003ca rel=\"nofollow\"\u003e             PMID:                        30201002            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR135a directly bound to UCA1 and the 3' untranslated region of cmyc, and UCA1 competed with cmyc for miR135a binding.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC directly regulates DANCR and plays important role in cancer cell proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29180471            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this review, we provide support to the hypothesis that the cooperation of c-Myc with transcriptional cofactors mediates c-Myc-induced cellular functions. We produce evidence that recently identified cofactors are involved in c-Myc control of survival mechanisms of cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        30261904            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            4-chlorobenzoyl berbamine (CBBM) inhibits the JAK2\/STAT3 pathway, leading to reduced c-Myc transcription. Collectively, these findings suggest that CBBM could be a promising lead compound for treatment of c-Myc-driven diffuse large B cell lymphoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30099568            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results revealed that C-MYC protein is highly expressed in colon cancer tissues, mainly in the cell nucleus and was identified as a direct target for mir-184. C-MYC appeared to participate in cell cycle regulation and malignant transformation to colon cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28782841            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MACC1 and c-Myc are highly expressed in serum and tumor tissues of EC patients. Both are correlated with TNM stage, primary infiltration, and lymph node or distal metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29984790            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study provides an interesting example using chemical biological approaches for determining distinct biological consequences from inhibiting vs. activating an E3 ubiquitin ligase and suggests a potential broad therapeutic strategy for targeting c-MYC in cancer treatment by pharmacologically modulating cIAP1 E3 ligase activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30181285            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The data demonstrated that 10058F4, a cMyc inhibitor, increased the growth inhibition, G0\/G1 phase arrest and apoptosis of the NALM6 and CEM cells as induced by dexamethasone (DXM), a type of GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749488            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-MYC\/BCL2 protein co-expression is associated with non-germinal center B-cell in Diffuse Large B-Cell Lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29801406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-Myc was capable of upregulating HP1gamma by directly binding to the E-box element in the first intron of HP1gamma gene, and the upregulated HP1gamma, in turn, repressed the expression of miR-451a by enhancing H3K9 methylation at the promoter region of miR-451a.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28967902            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A subset of pancreatic acinar cell carcinomas shows c-MYC alterations including gene amplification and chromosome 8 polysomy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29721608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression and Clinical Significance of LC-3 and P62 in Non-small Cell Lung Cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29945702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of the current study demonstrate presence of the IDH1 R132H mutation in primary human glioblastoma cell lines with upregulated HIF-1alpha expression, downregulating c-MYC activity and resulting in a consequential decrease in miR-20a, which is responsible for cell proliferation and resistance to standard temozolomide treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29625108            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a novel signal circuit of Stat3\/Oct-4\/c-Myc was identified for regulating stemness-mediated Doxorubicin resistance in triple-negative breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29750424            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC amplification and MYC overexpression occurred almost exclusively in secondary cutaneous angiosarcoma in our series.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29135507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with the development of prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29554906            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circular RNA hsa_circRNA_103809 promotes lung cancer progression via facilitating ZNF121-dependent MYC expression by sequestering miR-4302.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29698681            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors conclude that quantitative measurements of intratumor heterogeneity by multiplex FISH, detection of MYC amplification and TP53 mutation could augment prognostication in breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29181861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCYT1A was upregulated by MYC, which resulted in the induction of aberrant choline metabolism and the inhibition of B-lymphoma cell necroptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28686226            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cryptic t(3;8)(q27;q24) and\/or MYC-BCL6 linkage associated with MYC expression by immunohistochemistry is frequent in multiple-hit B-cell lymphomas.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28665415            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD30+ diffuse large B-cell lymphoma has characteristic clinicopathological features mutually exclusive with MYC gene rearrangement and negatively associated with BCL2 protein expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29666157            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High MYC amplification is associated with HER2 positive breast cancers in African American women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29523126            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest that MYC acts as a master coordinator that inversely modulates the impact of cell cycle and circadian clock on gene expression via its interaction with MIZ1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27339797            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In our study, the c-myc oncogene was amplified in 11.1% of BPH samples. Bivariate analysis failed to reveal any significant association between oncogene amplification and the clinicopathologic variables examined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29234244            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic variation at the 8q24.21 renal cancer susceptibility locus affects HIF1A and HIF1B binding to a MYC enhancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27774982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that miR-34a enhanced the sensitivity to cisplatin by upregulation of c-Myc and Bim pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29060932            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Luciferase reporter assay showed that c-Myc, an oncogene that regulating cell survival, angiogenesis and metastasis, was a direct target of miR-376a. Over-expression of miR-376a decreased the mRNA and protein levels of c-Myc in A549 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28741879            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present findings show that expression of c-MYC has prognostic value in squamous cell carcinoma of the tongue, and could be useful in choice of therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28393404            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Multivariable analysis indicated that IPI (P = 0.002), chemotherapy regimens (P = 0.017), and MYC gene rearrangements (P = 0.004) were independent adverse prognostic factors for all diffuse large B cell Lymphoma(DLBCL) patients in this study. Results demonstrated that the poor survival of DLBCL patients with HBV infection was closely involved in chemotherapy regimens, IPI, and MYC gene rearrangements            \u003ca rel=\"nofollow\"\u003e             PMID:                        29209623            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC extra copy in diffuse large B-cell lymphoma is an independent poor prognostic factor            \u003ca rel=\"nofollow\"\u003e             PMID:                        28776574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The c-Myc\/miR-200b\/PRDX2 loop regulates colorectal cancer (CRC) progression and its disruption enhances tumor metastasis and chemotherapeutic resistance in CRC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29258530            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998640406753,"sku":"BLC-02815P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP015270HU-SDS.jpg?v=1690502817"},{"product_id":"recombinant-mouse-myc-proto-oncogene-protein-myc-protein-gst-blc-02928p","title":"Recombinant Mouse Myc Proto-Oncogene Protein (MYC) Protein (GST)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Myc Proto-Oncogene Protein (MYC) Protein (GST) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 90% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P01108          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMyc; Myc proto-oncogene protein; Proto-oncogene c-Myc; Transcription factor p64\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMus musculus (Mouse)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-GST\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-439aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e76.0kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOthers\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTranscription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus, nucleoplasm. Nucleus, nucleolus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:17869           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000022971           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29249668            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            amino acid-controlled cMyc has an essential role in NK cell metabolism and function            \u003ca rel=\"nofollow\"\u003e             PMID:                        29904050            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Kidney specific MYC activation results in papillary clear cell renal cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28593993            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-Myc is essential for tumor initiation, maintenance, and metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29440228            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genomic characterization of Emu-Myc mouse lymphomas identifies Bcor as a Myc cooperative tumor-suppressor gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28262675            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The data supports an indispensable role for Mule in cardiac homeostasis through the regulation of mitochondrial function via maintenance of Pgc-1alpha and Pink1 expression and persistent negative regulation of c-Myc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28148912            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC binding is enriched at neuroendocrine genes in tumor cells and loss of MYC reduces ductal-neuroendocrine lineage heterogeneity, while deregulated MYC expression in KRAS mutants increases this phenotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29170413            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Although either BCR or CD40 ligation induced c-Myc in naive B cells, both signals were required to highly induce c-Myc, a critical mediator of GC B cell survival and cell cycle reentry.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29396161            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myc is a component that links neuromesodermal progenitors maintenance and pre-somitic mesoderm maturation during the body axis elongation stages of mouse embryogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30061166            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myc potentiates the Wnt\/beta-catenin signalling pathway, which cooperates with the transcriptional regulatory network in sustaining embryonic stem cell self-renewal.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27301576            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            clusters of enhancers, such as BENC in the myc gene, form highly combinatorial systems that allow precise control of gene expression across normal cellular hierarchies and which also can be hijacked in malignancies            \u003ca rel=\"nofollow\"\u003e             PMID:                        29342133            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Conditional deletion of Myc in hyaloid vascular endothelial cells suppressed both proliferation and cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29777010            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-Myc repression during development is crucial for the maturation of preacinar cells, and c-Myc overexpression can contribute to pancreatic carcinogenesis through the induction of a dedifferentiated state.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28159836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC negatively regulated the expression of genes involved in mitochondrial biogenesis and maintenance but positively regulated genes involved in DNA and histone methylation. Knockdown of MYC in colorectal cancer cells reset the altered metabolism and suppressed cell growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28847964            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High myc expression is associated with Intestinal Tumorigenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29533773            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results shed light on how overexpressed MYC alters the various phases of the RNAPII cycle and the resulting transcriptional response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28904013            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-Myc overexpression stimulated proliferation and activation of renal fibroblasts by inducing integrin alphav-mediated TGF-beta signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28483378            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the Myc-induced liver tumor model in zebrafish, a dramatic increase of liver size with neoplastic features was observed, as well as enhanced angiogenesis, and increase liver-infiltrated neutrophils and hypoxia. This model provides an excellent platform for study of tumor microenvironment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27549025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Using inducible genetic mosaics, we overexpressed Myc in the epicardium and determined the differential expansion of Myc-overexpressing cells with respect to their wild type counterparts. Myc-overexpressing cells overcolonized all epicardial-derived lineages and showed increased ability to invade the myocardium and populate the vasculature.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27752085            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nac1 overexpression promotes ESC proliferation and delays ESC differentiation in the absence of leukemia inhibitory factor (LIF). Furthermore, we demonstrated that Nac1 directly binds to the c-Myc promoter and regulates c-Myc transcription.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28548937            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study demonstrates that miR-451 regulates T cell proliferative responses in part via a Myc-dependent mechanism            \u003ca rel=\"nofollow\"\u003e             PMID:                        28378118            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AKAP1 is a transcriptional target of Myc, and it supports mTOR pathway and the growth of cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28569781            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with gliomagenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26993778            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the role of phosphorylation on AID serine38 in AID activity at the Immunoglobulin switch region and off-target Myc gene, is reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29122947            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrates that LMP2A uses the role of MYC in the cell cycle, particularly in the p27(kip1) degradation process, to accelerate lymphomagenesis in vivo.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29074502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show Myc to be dispensable for sustained in vivo hepatocyte proliferation but necessary for maintaining normal lipid homeostasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27105497            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Pin1 silencing in lymphomas retarded disease progression in mice, making Pin1 an attractive therapeutic target in Myc-driven tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26943576            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            beta-catenin cooperates with the transcription factor Myc to activate the progenitor renewal program.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28993399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gfi1 disruption antagonized the tumor-promoting effects of Ezh2 loss; conversely, Gfi1 overexpression collaborated with Myc to bypass effects of Trp53 inactivation in driving medulloblastoma progression in primary cerebellar neuronal progenitors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28329683            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            rather than via E-Box binding, cMyc acts in the dorsal neural tube by interacting with another transcription factor, Miz1, to promote self-renewal. The finding that cMyc operates in a non-canonical manner in the premigratory neural crest highlights the importance of examining its role at specific time points and in an in vivo context.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27926868            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-17-92-dependent tuning of LKB1 levels regulates both the metabolic potential of Myc+ lymphomas and tumor growth in vivo.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27498867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Under diabetic oxidative stress or H2O2 stimulation, nuclear beta-catenin accumulation upregulated downstream c-Myc and further facilitated DNA damage and p53-mediated apoptosis as well as cell viability reduction, followed by phenotypic changes of cardiac dysfunction, interstitial fibrosis deposition and myocardial atrophy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28989026            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            B-cell receptor controls fitness of MYC-driven lymphoma cells via GSK3beta inhibition            \u003ca rel=\"nofollow\"\u003e             PMID:                        28562582            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High Myc expression is associated with hepatocarcinogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28481866            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myc-high embryonic stem cells (ESCs) approach the naive pluripotency state, whereas Myc-low ESCs are closer to the differentiation-primed state.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28919206            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors here report the first MBG3 model from embryonic cerebellar cells by Myc activation and loss of Trp53 function using in utero electroporation (EP)-based in vivo gene transfer combined to a Cre\/LoxP-mediated technology.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28504719            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            by controlling both nanodomain decompaction and PolII promoter escape Myc stands as a master regulator of transcriptome amplification during B cell activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28803781            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results indicate that PIAS1 is a positive regulator of MYC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27239040            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that that deletion of Sox2 increases the frequency of IgH:c-Myc translocations            \u003ca rel=\"nofollow\"\u003e             PMID:                        28188246            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings highlight a MYC\/ERRalpha pathway that contributes to physiological and pathological bone loss by integrating the MYC\/ERRalpha axis to drive metabolic reprogramming during osteoclast differentiation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28530645            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that Emu-Myc mice lacking both p21 and PUMA developed lymphoma at a rate considerably longer latency than Emu-Myc;p53(+\/-)mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26640149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CRY2 and FBXL3 cooperatively degrade c-MYC preventing the development of cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27840026            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data, including data from studies in cells from knockout mice, suggest that Prmt1 activity was necessary for c-Myc binding to acetyltransferase p300 in myeloid cells; Prmt1 inhibition decreases p300 recruitment to c-Myc target promoters and increased Hdac1 recruitment. [Prmt1, protein arginine N-methyltransferase 1; c-Myc = Proto-Oncogene Proteins c-myc; Hdac1 = histone deacetylase 1]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28652407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC-dependent attenuation of GCLC by miR-18a contributes to GSH depletion in vivo, and low GSH corresponds with increased sensitivity to oxidative stress in tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28219903            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC mediates cell cycle re-entry of Trp53-altered hepatocytes via AURKA binding.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27213815            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myc can substitute for Notch1 in leukemogenesis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27670423            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results show how MYC drives the production of specific eicosanoids critical for lung cancer cell survival and proliferation            \u003ca rel=\"nofollow\"\u003e             PMID:                        27335109            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Early generated B1 B cells with restricted BCRs become chronic lymphocytic leukemia with continued c-Myc and low Bmf expression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27899442            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data (including data from studies using transgenic mice) suggest that expression of c-Myc in liver can be correlated with progression, regression, and recurrence of hepatocellular carcinoma (using a specific mouse model).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28432125            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TCF7L2 mediates canonic Wnt\/beta-catenin signaling and c-Myc upregulation during abnormal cardiac remodeling in heart failure and suppression of Wnt\/beta-catenin to c-Myc axis can be explored for preventing and treating heart failure.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27301468            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998651449569,"sku":"BLC-02928P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP015270MO-SDS.jpg?v=1690503189"},{"product_id":"recombinant-human-n-myc-proto-oncogene-protein-mycn-protein-his-blc-03319p","title":"Recombinant Human N-Myc Proto-Oncogene Protein (MYCN) Protein (His)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human N-Myc Proto-Oncogene Protein (MYCN) Protein (His) is produced by our Yeast expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 90% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P04198          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYCN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ebHLHe37; Class E basic helix-loop-helix protein 37; MODED; mycn; MYCN_HUMAN; N myc; N myc proto oncogene protein; N-myc proto-oncogene protein; Neuroblastoma derived v myc avian myelocytomatosis viral related oncogene; Neuroblastoma MYC oncogene; NMYC; NMYC proto oncogene protein; ODED; Oncogene NMYC; pp65\/67; V myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog; v myc avian myelocytomatosis viral related oncogene neuroblastoma derived; v myc myelocytomatosis viral related oncogene neuroblastoma derived\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eYeast\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-6His\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-464aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e51.6kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCancer\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePositively regulates the transcription of MYCNOS in neuroblastoma cells.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7559           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            164280           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4613           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000281043           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30451831            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            This suggested that NMyc regulated survival and growth of CHP134 and BE2C neuroblastoma cells, potentially through Wnt\/betacatenin signaling. Furthermore, associated proteins, NMyc and STAT interactor and dickkopf Wnt signaling pathway inhibitor 1, were demonstrated to be involved in this regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749516            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this report, we present a case with Feingold Syndrome having a novel mutation in MYCN gene and discuss genetic counselling and prenatal diagnosis due to pregnancy of the patient's mother.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30204967            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results demonstrated that MYCN expression was downregulated in cholangiocarcinoma (CCA) through a mechanism involving miR-5095 binding its 3'UTR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29620172            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN levels are regulated transcriptionally by MYCNOS-01 (an alternative transcript of MYCNOS) in rhabdomyosarcoma and neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29466962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a MycN\/CIP2A-mediated cell-fate bias may reflect a possible mechanism underlying early priming of some aggressive forms of neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30021854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD133 expression and MYCN amplification induce chemoresistance and reduce average survival time in pediatric neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29322842            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that inter-play between MYCN and the highly tumorigenic proteins which are upregulated in the malignant IMR-32 neuroblastoma cells may be fueling their aggressive behavior.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29328367            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results suggest that MYCN serves as a prognostic biomarker and therapeutic target of ACR for liver cancer stem cell in de novo Hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29686061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Alternative nonhomologous DNA end-joining pathway proteins as components of MYCN oncogenic activity in human neural crest stem cell differentiation have been revealed in the process of neuroblastoma initiation in mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29238067            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TrkA expression is one of the most powerful predictor of good prognosis in neuroblastoma and is associated with younger age, lower stage, and absence of MYCN amplification            \u003ca rel=\"nofollow\"\u003e             PMID:                        29018959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of MYCN promoted cell proliferation, and induced erythroid differentiation block and apoptosis resistance to cytotoxic agent.  Knockdown of MYCN inhibited the expression of EZH2, and then activated p21 expression through removal of H3K27me3 at the p21 promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29022893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MAX to MYCN ratio that can account for tumour progression and clinical outcome in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29408445            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN expression is regulated by ZAR1 in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28791558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The target of miR-29b was predicted using miRanda, TargetScan and PicTar sofeware and authors also found MYCN was a direct target of miR-29b in glioma cells and miR-29b inhibited the proliferation of glioma cells via MYCN dependent way.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28423357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            eEF2K protects MYCN overexpressing NB cells from ND in vitro and in vivo, highlighting this kinase as a critical mediator of the adaptive response of MYCN amplified NB cells to metabolic stress.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574509            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Among 30 samples of brain tumor, 14 cases revealed MYCN amplification. High-protein expression of MYCN was also observed in 43.3% of patients. There was a significant correlation between MYCN gene amplification and protein expression, interestingly five case showed discrepancy between the gene amplification and protein expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28453467            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PRMT1 has a role in regulating MYCN in neuroblastoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27571165            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            N-myc levels appear to be modulated by the antagonistic interactions of both miR-17, as a negative regulator, and HuD, as a positive regulator in N-myc-amplified neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28560387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We also propose a model for the stabilization mechanism in which binding to Aurora-A alters how N-Myc interacts with SCF(FbxW7) to disfavor the generation of Lys48-linked polyubiquitin chains            \u003ca rel=\"nofollow\"\u003e             PMID:                        27837025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study provides a novel insight for miR-221 in the control of neuroblastoma cell proliferation and tumorigenesis, suggesting potentials of miR-221 as a prognosis marker and therapeutic target for patients with MYCN overexpressing neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28003306            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            N-MYC is in the downstream-regulated gene family in reprogramming cancer metabolism under hypoxia [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27447861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNHG1 is up-regulated by MYCN amplification and could be a potential prognostic biomarker for high-risk neuroblastoma intervention.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27517149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN expression is a marker indicative of likely clinical sensitivity to mTOR inhibition in neuroblastoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27438153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that MYCN and LSD1 co-localize at NDRG1 promoter and repress its expression in neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27894074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate cross-talks between MYCN and beta-catenin signalling, which repress normal beta-catenin mediated transcriptional regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27531891            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that transcription factor activating enhancer binding protein-4 (TFAP4) is a direct transcriptional target of MYCN in neuroblastoma and that high levels of this transcription factor are associated with poor clinical outcome in this disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27448979            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data extend knowledge on roles of MCPIP1 in our model and link the protein to regulation of expression and stability of MYCN through decrease of signaling via Akt\/mTOR pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27935099            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that MYCN and its regulated microRNAs acted together to repress the tumor suppressor genes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27167114            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Common genetic variation predisposes to different neuroblastoma genotypes, including the likelihood of somatic MYCN-amplification. [meta-analysis]            \u003ca rel=\"nofollow\"\u003e             PMID:                        29117357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results establish evidence that high MYCN amplification can be present in retinoblastoma with or without coding sequence mutations in the RB1 gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28211617            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study conducted metabolic profiling of pre-malignant sympathetic ganglia and tumors derived from the TH-MYCN mouse model of neuroblastoma, that overexpresses human MYCN and compared to non-malignant ganglia from wildtype littermates. These results identify enhanced glutathione biosynthesis as a selective metabolic adaptation required for initiation of MYCN-driven neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26996379            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many prognostic signatures for neuroblastoma are confounded by MYCN amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27599694            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increasing MYCN copy number is associated with an increasingly higher rate of unfavorable clinical\/biological features, with 11q aberration being an exception. Patients with MYCN gain appear to have inferior outcomes, especially in otherwise more favorable groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28696504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-21 enhances chemo-resistance in tongue cancer cells via directly targeting CADM1, and an inverse correlation between miR-21 and CADM1 expression in vivo. MiR-21 overexpression is attributed to MYCN-mediated transcriptional regulation, which is also predictive for a worse prognosis in tongue cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27055844            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LMO1 is an important oncogene that promotes neuroblastoma initiation, progression, and widespread metastatic dissemination.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867147            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results identify DOT1L as a novel cofactor in N-Myc-mediated transcriptional activation of target genes and neuroblastoma oncogenesis. Furthermore, they characterize DOT1L inhibitors as novel anticancer agents against MYCN-amplified neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28209620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CCCTC-binding factor (CTCF) targets the binding sites within MYCN promoter to facilitate its expression in neuroblastoma (NB) cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26549029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PAX3-FOXO1 collaborates with MYCN during early rhabdomyosarcoma (RMS) tumourigenesis to dysregulate proliferation and inhibit myogenic differentiation and cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28138962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings reveal a PLK1-Fbw7-Myc signaling circuit that underlies tumorigenesis and validate PLK1 inhibitors, alone or with Bcl2 antagonists, as potential effective therapeutics for MYC-overexpressing cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27773673            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that N-Myc overexpression leads to the development of poorly differentiated, invasive prostate cancer that is molecularly similar to human NEPC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27728805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Rac activity may be an important determinant of metastatic capability in subsets of neuroblastoma cells lacking MYCN amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27224546            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN Gene Amplification is associated with Neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27513929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN overexpression combined with activated anaplastic lymphoma kinase (ALK) is sufficient to induce neuroblastoma (NB) in mouse sympathoadrenal cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27707976            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN amplification can be heterogeneous between tumor sites, during tumor progression or following treatment, challenging the notion that MYCN copy number does not change for a particular neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27465929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High MycN expression is associated with low radiosensitivity in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27432152            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            applying loss-and-gain function analysis, we demonstrated that miR-34a directly targeted to MYCN to sensitize NSCLC cells to cisplatin. In addition, p53 was found to monitor the expression of miR-34a in NSCLC cells after cisplatin treatment. Therefore, the sensitivity of cisplatin in NSCLC cells was modulated via p53\/miR-34a\/MYCN axis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27836543            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data supports our hypothesis that a positive-feedback loop of sonic hedgehog signaling induced INSM1 through N-myc and INSM1 enhanced N-myc stability contributing to the transformation of human neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26456864            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog (MYCN) was overexpressed in non-small cell lung cancer (NSCLC) tumor tissues and cell lines, suggesting that targeting MYCN might provide beneficial effects for the clinical therapy of NSCLC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27449038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            That initial decision to deny coverage could have had untoward health implications for this child, as the identification of constitutional MYCN duplication necessitated surveillance imaging for a number of pediatric malignancies associated with MYCN            \u003ca rel=\"nofollow\"\u003e             PMID:                        27794475            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998686019809,"sku":"BLC-03319P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-YP015278HU-SDS.jpg?v=1690504398"},{"product_id":"recombinant-mouse-peroxisomal-acyl-coenzyme-a-oxidase-1-acox1-protein-myc-blc-04855p","title":"Recombinant Mouse Peroxisomal Acyl-Coenzyme A Oxidase 1 (ACOX1) Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Peroxisomal Acyl-Coenzyme A Oxidase 1 (ACOX1) Protein (Myc) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           Q9R0H0          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eACOX1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAcox1; Acox; PaoxPeroxisomal acyl-coenzyme A oxidase 1; AOX; EC 1.3.3.6; Palmitoyl-CoA oxidase) [Cleaved into: Peroxisomal acyl-CoA oxidase 1; A chain; Peroxisomal acyl-CoA oxidase 1; B chain; Peroxisomal acyl-CoA oxidase 1; C chain]\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMus musculus (Mouse)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eC-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMNPDLRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREFGIADPEEIMWFKKLHMVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQSGKLVGGMVSYLNDLPSQRIQPQQVAVWPTLVDINSLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWAKKSPLNKTEVHESYYKHLKPLQSKL\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-661aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e76.2 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCancer\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCatalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.; Shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length.; Is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePeroxisome.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAcyl-CoA oxidase family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:11430           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000063325           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        22521832            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            progressive PPARalpha- and p8-mediated ER stress contribute to the hepatocarcinogenesis in ACOX1(-\/-) mice            \u003ca rel=\"nofollow\"\u003e             PMID:                        21801867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Loss of Fatty acyl-CoA oxidase leads to increased amounts of PPARalpha, peroxisomal bifunctional enzyme and thiolase in hepatocellular carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        12429965            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            STAT5A binds to -1841 to -1825 of the murine AOX promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16650827            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998864113889,"sku":"BLC-04855P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP882598MO-SDS.jpg?v=1690509280"},{"product_id":"recombinant-rat-mast-cell-protease-1-mcpt1-protein-myc-blc-05255p","title":"Recombinant Rat Mast Cell Protease 1 (MCPT1) Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Rat Mast Cell Protease 1 (MCPT1) Protein (Myc) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P09650          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMCPT1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMcpt1Mast cell protease 1; rMCP-1; EC 3.4.21.39; Chymase; Chymotrypsin-like protease; CLIP protein; Mast cell protease I; rMCP-I\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRattus norvegicus (Rat)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eIIGGVESRPHSRPYMAHLEITTERGYKATCGGFLVTRQFVMTAAHCKGRETTVTLGVHDVSKTESTQQKIKVEKQIVHPNYNFYSNLHDIMLLKLQKKAKVTPAVDVIPLPQPSDFLKPGKMCRAAGWGQTGVTKPTSNTLREVKQRIMDKEACKNYFHYNYNFQVCVGSPRKIRSAYKGDSGGPLVCAGVAHGIVSYGRGDAKPPAVFTRISPYVPWINKVIKGKDLTSLSLHESESPS\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e21-260aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length of Mature Protein\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e28.6 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCancer\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMajor secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. May participate in generating perivascular beta-protein which ultimately aggregates into amyloid-beta deposits.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Cytoplasmic granule.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePeptidase S1 family, Granzyme subfamily\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            rno:100360872           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10116.ENSRNOP00000028012           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/UniGene\/clust.cgi?ORG=Rn\u0026amp;CID=145977\"\u003e            Rn.145977           \u003c\/a\u003e \u003c\/p\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43998909268193,"sku":"BLC-05255P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP357723RA-1.jpg?v=1690566258"},{"product_id":"recombinant-human-brain-derived-neurotrophic-factor-bdnf-protein-myc-blc-06141p","title":"Recombinant Human Brain-Derived Neurotrophic Factor (BDNF) Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Brain-Derived Neurotrophic Factor (BDNF) Protein (Myc) is produced by our E.coli expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 90% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P23560          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBDNF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19-247aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25.8 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCardiovascular\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eImportant signaling molecule that activates signaling cascades downstream of NTRK2. During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.; Important signaling molecule that activates signaling cascades downstream of NTRK2. Activates signaling cascades via the heterodimeric receptor formed by NGFR and SORCS2. Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and long-term depression (LTD). Binding to NGFR and SORCS2 promotes neuronal apoptosis. Promotes neuronal growth cone collapse.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.; [BDNF precursor form]: Secreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            1033           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            113505           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:627           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000414303           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29734216            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Low brain derived neurotrophic factor may contribute to the pathogenesis of schizophrenia, but maybe not to its cognitive impairments.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29482040            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In a 12-year longitudinal population-based sample of older adults (n = 2,218), we used growth curve modeling to investigate whether the benefits of physical activity on cognitive preservation differed by BDNF genotype and sex across multiple cognitive domains including processing speed, attention, working memory, and episodic verbal memory.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29402782            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mn-SOD V allele carries a worse outcome profile after stroke, relating to nitrosative stress, inflammatory, and apoptotic response and associated with a BDNF reduction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30150066            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            while the BDNF Val66Met Megroup displayed significant SICI reduction in the bilateral M1 in response to motor training, short-interval intracortical inhibition (SICI) remained unchanged in the BDNF Val66Met group.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29856758            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study provides evidence for the correlation between the BDNF variant rs6265 and emotional symptoms in the early phase after mild traumatic brain injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29357818            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicate that genetic variant Met66 decreased the serum BDNF levels in combination with self-reported risk-taking propensity among heroin users.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30134233            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum BDNF levels and the BDNF Val66Met polymorphism in healthy young adults were associated with the sleep pattern on weekends but not with that on weekdays, suggesting that the systems involved in BDNF control may be linked to endogenous sleep characteristics rather than the socially constrained sleep schedule in healthy young adults.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29944703            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neurotrophic factors and hippocampal activity in PTSD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29799860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            upregulation of PAI-1 may be a critical mechanism underlying insufficient neurotrophic support and increased neurodegeneration associated with AD. Thus, targeting BDNF maturation through pharmacological inhibition of PAI-1 might become a potential treatment for AD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28132883            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study shows the genetic correlates of early trauma in a group of schizophrenia patients (BDNF Met carriers).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28711474            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated significant differences in the blood levels of BDNF between people with epilepsy and healthy subjects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30140987            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows that brain-derived neurotrophic factor concentrations in serum and peritoneal fluid were significantly higher in women with endometriosis with pain compared to women with endometriosis without pain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28954602            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Met allele of the Val66Met polymorphism in brain derived neurotrophic factor is associated with lower BMI-SDS in children            \u003ca rel=\"nofollow\"\u003e             PMID:                        28960774            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            platelet BDNF and SERT do not specifically underlie psychosocial deficits in stage Huntington's Disease, while higher BDNF storage in delayed mild symptoms            \u003ca rel=\"nofollow\"\u003e             PMID:                        30039833            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Direct within family analysis showed that fathers with the Met allele were more likely than Val\/Val carriers to exhibit differential parenting toward twins who differed in their prosocial behavior. The same pattern of findings was found with mother-rated and experimentally assessed prosociality.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28523227            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that the Val66Met polymorphism does not predict long-term, functional mobility following stroke.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29480080            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            polymorphisms in BDNF gene including rs925946, rs10501087, rs6265 and rs988712 can be considered as genetic determinants of obesity (systematic review and meta-analysis).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28818748            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Single nucleotide polymorphism found in the BDNF-AS (BDNF antisense RNA [nonprotein coding]) gene may be related to the decreased plasma brain derived neurotrophic factor levels found in frail elderly people.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27449141            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The pattern of low BDNF and high inflammation in MDD may be influenced by the Val66Met polymorphism; the association of a polymorphism in the BDNF gene with inflammatory markers in addition to BDNF levels suggests an interaction between these systems.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28656803            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Angiogenin contributes to angiogenesis induced by Brain-derived neurotrophic factor (BDNF).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29573867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings demonstrated that polymorphism Val66Met is not associated with temporal lobe epilepsy caused by hippocampal sclerosis, epilepsy-related factors and psychiatric comorbidities in this selected group of patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015148            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study suggested that BDNF 196 G\u0026gt;A polymorphism may be a genetic marker for predicting insulin resistance before initiating risperidone treatment in autism spectrum disorder patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29369497            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No significant difference was found in the BDNF Val66Met polymorphism between patients with GAD and healthy controls, nor was this polymorphism significantly associated with antidepressant drug efficacy for GAD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29446659            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Its single-nucleotide polymorphisms involves in dopaminergic metabolism and motor and cognitive function in older adults.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29525179            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF rs11030101 and BDNF rs61888800are associated with change of temperament scores in a clinical sample of subjects with major depression (MDD), who received selective serotonin reuptake inhibitor treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29310728            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found that harsh parenting predicted an increased error-related negativity only among children with a methionine allele of the BDNF genotype, and evidence of moderated mediation: the ERN mediated the relationship between parenting and internalizing diagnoses and dimensional symptoms only if children had a methionine allele.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28427482            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings presented here suggest a strong influence of seasonality on depression outcome and BDNF expression in atopic dermatitis and psoriasis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27409526            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum BDNF was significantly lower in patients with Parkinson's disease than in patients with essential tremor and controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29350074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The purpose of this systematic review was to provide a comprehensive analysis of the available clinical trials analyzing, in seniors, the effect of interval aerobic training (IAT) and continuous aerobic training (CAT) on peripheral brain-derived neurotrophic factor (BDNF) concentration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28498065            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggested that BDNF modulates graunlosa cell functions and the action probably mediated by FSHR-coupled signaling pathway, to affect aromatase-mediated steroidogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28282971            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The functional Val66Met BDNF polymorphism is not associated with BDNF serum levels in acute episode of schizophrenia and depression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29331787            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated that a significantly higher incidence of defective BDNF expression in granule layers of the cerebellar cortex.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29174061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            combining cognitive and physical exercise had no additional or synergistic effect on peripheral BDNF levels compared with physical exercise alone            \u003ca rel=\"nofollow\"\u003e             PMID:                        29842831            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Review\/Meta-analysis: suggests a lower risk of ischemic stroke for the GG genotype of BDNF rs6265.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29449128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that the BDNF SNP rs1157659 interacted with mild traumatic brain injury to predict hippocampal volume            \u003ca rel=\"nofollow\"\u003e             PMID:                        28755387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            found that though there was no significantly difference in peripheral BDNF levels between ADHD patients and control groups overall, BDNF levels were significantly higher in males with ADHD compared with controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29132072            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            found evidence that supported the hypothesis that BDNF Val66Met polymorphism moderated the relationship between stress and depression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29102837            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the BDNF Val66Met polymorphism is associated with functional tuning of behaviorally-relevant frontolimbic circuitry, particularly involving the ventromedial prefrontal cortex, during higher-order learning.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867340            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MicroRNA-103 suppresses glioma cell proliferation and invasion by targeting BDNF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29257320            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression levels of BDNF was observed in cervical cancer.BDNF role in epithelial-mesenchymal transition, migration and invasion of cervical cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29345295            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was a statistically significant change in BDNF levels post-chemotherapy in early-stage breast cancer patients, and plasma BDNF levels were associated with self-perceived concentration deficit in patients receiving chemotherapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29258453            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Meta-analysis\/Review: patients with ischemic stroke at high risk of post stroke depression have lower BDNF levels at the early stage of stroke.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29128330            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Coronary artery disease patients exhibited significantly lower plasma BDNF and higher vWF levels than those of control patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29409455            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Brain-derived neurotrophic factor (BDNF) was found to be the downstream target of miR-107 in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27813254            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study showed that in first-episode psychosis subjects, with global DNA hypo-methylation and reduced BDNF gene-expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29056292            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            down-regulated in cord blood by prenatal smoking            \u003ca rel=\"nofollow\"\u003e             PMID:                        28130959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF\/TrkB axis plays a role in epithelial mesenchymal transition promoting the acquisition of (myo)fibroblast cell phenotype in idiopathic pulmonary fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28938915            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that Lnc RNA BDNF-AS inversely regulates the expression level of BDNF which modulates high-glucose induced apoptosis in human retinal pigment epithelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28657668            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study show a linear relationship between the BDNF Val66Met genotypes and plasma BDNF levels in Caucasian depressed patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28848102            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43999000068321,"sku":"BLC-06141P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP002655HU_A4_-SDS.jpg?v=1690512968"},{"product_id":"recombinant-human-n-myc-proto-oncogene-protein-mycn-protein-his-blc-06605p","title":"Recombinant Human N-Myc Proto-Oncogene Protein (MYCN) Protein (His)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human N-Myc Proto-Oncogene Protein (MYCN) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 90% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P04198          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYCN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e(Class E basic helix-loop-helix protein 37)(bHLHe37)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBaculovirus\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eC-6His\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-464aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e52.4 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCancer\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePositively regulates the transcription of MYCNOS in neuroblastoma cells.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7559           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            164280           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4613           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000281043           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30451831            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            This suggested that NMyc regulated survival and growth of CHP134 and BE2C neuroblastoma cells, potentially through Wnt\/betacatenin signaling. Furthermore, associated proteins, NMyc and STAT interactor and dickkopf Wnt signaling pathway inhibitor 1, were demonstrated to be involved in this regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749516            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this report, we present a case with Feingold Syndrome having a novel mutation in MYCN gene and discuss genetic counselling and prenatal diagnosis due to pregnancy of the patient's mother.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30204967            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results demonstrated that MYCN expression was downregulated in cholangiocarcinoma (CCA) through a mechanism involving miR-5095 binding its 3'UTR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29620172            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN levels are regulated transcriptionally by MYCNOS-01 (an alternative transcript of MYCNOS) in rhabdomyosarcoma and neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29466962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a MycN\/CIP2A-mediated cell-fate bias may reflect a possible mechanism underlying early priming of some aggressive forms of neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30021854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD133 expression and MYCN amplification induce chemoresistance and reduce average survival time in pediatric neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29322842            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that inter-play between MYCN and the highly tumorigenic proteins which are upregulated in the malignant IMR-32 neuroblastoma cells may be fueling their aggressive behavior.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29328367            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results suggest that MYCN serves as a prognostic biomarker and therapeutic target of ACR for liver cancer stem cell in de novo Hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29686061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Alternative nonhomologous DNA end-joining pathway proteins as components of MYCN oncogenic activity in human neural crest stem cell differentiation have been revealed in the process of neuroblastoma initiation in mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29238067            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TrkA expression is one of the most powerful predictor of good prognosis in neuroblastoma and is associated with younger age, lower stage, and absence of MYCN amplification            \u003ca rel=\"nofollow\"\u003e             PMID:                        29018959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of MYCN promoted cell proliferation, and induced erythroid differentiation block and apoptosis resistance to cytotoxic agent.  Knockdown of MYCN inhibited the expression of EZH2, and then activated p21 expression through removal of H3K27me3 at the p21 promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29022893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MAX to MYCN ratio that can account for tumour progression and clinical outcome in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29408445            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN expression is regulated by ZAR1 in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28791558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The target of miR-29b was predicted using miRanda, TargetScan and PicTar sofeware and authors also found MYCN was a direct target of miR-29b in glioma cells and miR-29b inhibited the proliferation of glioma cells via MYCN dependent way.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28423357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            eEF2K protects MYCN overexpressing NB cells from ND in vitro and in vivo, highlighting this kinase as a critical mediator of the adaptive response of MYCN amplified NB cells to metabolic stress.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574509            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Among 30 samples of brain tumor, 14 cases revealed MYCN amplification. High-protein expression of MYCN was also observed in 43.3% of patients. There was a significant correlation between MYCN gene amplification and protein expression, interestingly five case showed discrepancy between the gene amplification and protein expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28453467            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PRMT1 has a role in regulating MYCN in neuroblastoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27571165            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            N-myc levels appear to be modulated by the antagonistic interactions of both miR-17, as a negative regulator, and HuD, as a positive regulator in N-myc-amplified neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28560387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We also propose a model for the stabilization mechanism in which binding to Aurora-A alters how N-Myc interacts with SCF(FbxW7) to disfavor the generation of Lys48-linked polyubiquitin chains            \u003ca rel=\"nofollow\"\u003e             PMID:                        27837025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study provides a novel insight for miR-221 in the control of neuroblastoma cell proliferation and tumorigenesis, suggesting potentials of miR-221 as a prognosis marker and therapeutic target for patients with MYCN overexpressing neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28003306            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            N-MYC is in the downstream-regulated gene family in reprogramming cancer metabolism under hypoxia [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27447861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNHG1 is up-regulated by MYCN amplification and could be a potential prognostic biomarker for high-risk neuroblastoma intervention.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27517149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN expression is a marker indicative of likely clinical sensitivity to mTOR inhibition in neuroblastoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27438153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that MYCN and LSD1 co-localize at NDRG1 promoter and repress its expression in neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27894074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate cross-talks between MYCN and beta-catenin signalling, which repress normal beta-catenin mediated transcriptional regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27531891            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that transcription factor activating enhancer binding protein-4 (TFAP4) is a direct transcriptional target of MYCN in neuroblastoma and that high levels of this transcription factor are associated with poor clinical outcome in this disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27448979            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data extend knowledge on roles of MCPIP1 in our model and link the protein to regulation of expression and stability of MYCN through decrease of signaling via Akt\/mTOR pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27935099            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that MYCN and its regulated microRNAs acted together to repress the tumor suppressor genes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27167114            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Common genetic variation predisposes to different neuroblastoma genotypes, including the likelihood of somatic MYCN-amplification. [meta-analysis]            \u003ca rel=\"nofollow\"\u003e             PMID:                        29117357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results establish evidence that high MYCN amplification can be present in retinoblastoma with or without coding sequence mutations in the RB1 gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28211617            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study conducted metabolic profiling of pre-malignant sympathetic ganglia and tumors derived from the TH-MYCN mouse model of neuroblastoma, that overexpresses human MYCN and compared to non-malignant ganglia from wildtype littermates. These results identify enhanced glutathione biosynthesis as a selective metabolic adaptation required for initiation of MYCN-driven neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26996379            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many prognostic signatures for neuroblastoma are confounded by MYCN amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27599694            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increasing MYCN copy number is associated with an increasingly higher rate of unfavorable clinical\/biological features, with 11q aberration being an exception. Patients with MYCN gain appear to have inferior outcomes, especially in otherwise more favorable groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28696504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-21 enhances chemo-resistance in tongue cancer cells via directly targeting CADM1, and an inverse correlation between miR-21 and CADM1 expression in vivo. MiR-21 overexpression is attributed to MYCN-mediated transcriptional regulation, which is also predictive for a worse prognosis in tongue cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27055844            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LMO1 is an important oncogene that promotes neuroblastoma initiation, progression, and widespread metastatic dissemination.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867147            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results identify DOT1L as a novel cofactor in N-Myc-mediated transcriptional activation of target genes and neuroblastoma oncogenesis. Furthermore, they characterize DOT1L inhibitors as novel anticancer agents against MYCN-amplified neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28209620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CCCTC-binding factor (CTCF) targets the binding sites within MYCN promoter to facilitate its expression in neuroblastoma (NB) cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26549029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PAX3-FOXO1 collaborates with MYCN during early rhabdomyosarcoma (RMS) tumourigenesis to dysregulate proliferation and inhibit myogenic differentiation and cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28138962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings reveal a PLK1-Fbw7-Myc signaling circuit that underlies tumorigenesis and validate PLK1 inhibitors, alone or with Bcl2 antagonists, as potential effective therapeutics for MYC-overexpressing cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27773673            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that N-Myc overexpression leads to the development of poorly differentiated, invasive prostate cancer that is molecularly similar to human NEPC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27728805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Rac activity may be an important determinant of metastatic capability in subsets of neuroblastoma cells lacking MYCN amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27224546            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN Gene Amplification is associated with Neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27513929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN overexpression combined with activated anaplastic lymphoma kinase (ALK) is sufficient to induce neuroblastoma (NB) in mouse sympathoadrenal cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27707976            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN amplification can be heterogeneous between tumor sites, during tumor progression or following treatment, challenging the notion that MYCN copy number does not change for a particular neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27465929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High MycN expression is associated with low radiosensitivity in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27432152            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            applying loss-and-gain function analysis, we demonstrated that miR-34a directly targeted to MYCN to sensitize NSCLC cells to cisplatin. In addition, p53 was found to monitor the expression of miR-34a in NSCLC cells after cisplatin treatment. Therefore, the sensitivity of cisplatin in NSCLC cells was modulated via p53\/miR-34a\/MYCN axis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27836543            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data supports our hypothesis that a positive-feedback loop of sonic hedgehog signaling induced INSM1 through N-myc and INSM1 enhanced N-myc stability contributing to the transformation of human neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26456864            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog (MYCN) was overexpressed in non-small cell lung cancer (NSCLC) tumor tissues and cell lines, suggesting that targeting MYCN might provide beneficial effects for the clinical therapy of NSCLC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27449038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            That initial decision to deny coverage could have had untoward health implications for this child, as the identification of constitutional MYCN duplication necessitated surveillance imaging for a number of pediatric malignancies associated with MYCN            \u003ca rel=\"nofollow\"\u003e             PMID:                        27794475            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43999058854113,"sku":"BLC-06605P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-BP015278HUc7-SDS.jpg?v=1690514779"},{"product_id":"recombinant-mouse-epithelial-cell-adhesion-molecule-epcam-protein-myc-blc-07570p","title":"Recombinant Mouse Epithelial Cell Adhesion Molecule (EPCAM) Protein (Myc)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Epithelial Cell Adhesion Molecule (EPCAM) Protein (Myc) is produced by our Mammalian cell expression system. This is a protein fragment.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           Q99JW5          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEPCAM\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e(Ep-CAM)(Epithelial glycoprotein 314)(EGP314)(mEGP314)(Protein 289A)(Tumor-associated calcium signal transducer 1)(CD antigen CD326)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMus musculus (Mouse)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMammalian cell\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eC-Myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQRDCVCDNYKLATSCSLNEYGECQCTSYGTQNTVICSKLASKCLAMKAEMTHSKSGRRIKPEGAIQNNDGLYDPDCDEQGLFKAKQCNGTATCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKERESPYDHQSLQTALQEAFTSRYKLNQKFIKNIMYENNVITIDLMQNSSQKTQDDVDIADVAYYFEKDVKGESLFHSSKSMDLRVNGEPLDLDPGQTLIYYVDEKAPEFSMQGLT\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e24-266aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePartial\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e29.5 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCell-Cell Adhesion\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMay act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLateral cell membrane; Single-pass type I membrane protein. Cell junction, tight junction.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEPCAM family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:17075           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000061935           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29958886            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            EpEX\/EpCAM are sufficient to reprogram fibroblasts into iPSCs with only Oct4 or Klf4.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28157205            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            extracellular vesicles tend to localize in the intestinal tract associated with epithelial cell adhesion molecule            \u003ca rel=\"nofollow\"\u003e             PMID:                        27721471            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that EpCAM-expressing proliferating ductal cells (PDC) could be a cellular origin of hepatocellular carcinoma (HCC), suggesting the existence of stem\/progenitor-derived hepatocarcinogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28951464            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            activation of hepatic H19RNA promoted cholestatic liver fibrosis through the ZEB1\/EpCAM signaling pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        28407375            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results identify EpCAM as a substrate of matriptase and link HAI-2, matriptase, EpCAM, and claudin-7 in a functionally important pathway that causes disease when it is dysregulated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28094766            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM appears to differentially regulate Langerhans cell mobility\/migration in the setting of limited inflammation as compared with the intense inflammation triggered by contact sensitizers            \u003ca rel=\"nofollow\"\u003e             PMID:                        27106675            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Knock-down EpCAM cell model of congenital tufting enteropathy was developed. In vivo inducible mouse model was developed resulting in mutant EpCAM protein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25482158            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            in addition to converting to cholangiocyte-like cells, Sox9(+)EpCAM(-) cells provide luminal space near expanded ductular structures to prevent deterioration of the injuries and potentially supply new hepatocytes to repair damaged tissues            \u003ca rel=\"nofollow\"\u003e             PMID:                        24482234            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM is a highly conserved protein present in fishes, amphibians, reptiles, birds, marsupials, and placental mammals, and is subject to shedding, gamma-secretase-dependent regulated intramembrane proteolysis, and proteasome-mediated degradation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24009667            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suggest pivotal role of EpCAM in intestinal epithelial structure and integrity, with mutations resulting in congenital tufting enteropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24337010            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            mTrop1\/Epcam knockout mice develop congenital tufting enteropathy through dysregulation of intestinal E-cadherin\/beta-catenin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23209569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM contributes to formation of intestinal barrier by recruiting claudins to cell-cell junctions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22819673            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results conclusively link EpCAM expression to Langerhan cell (LC) motility\/migration and LC migration to immune regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22411813            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that SSCs are the most concentrated in CD9(+)EPCAM(low\/-) population and also suggest that EPCAM plays an important role in progenitor cell amplification in the mouse spermatogenic system.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21858196            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM could contribute substantially to the pathogenesis of lung cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21535318            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM was required for differentiation or survival of parietal trophoblast giant cells, normal development of the placental labyrinth and establishment of a competent maternal-fetal circulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20046825            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of EpCAM expression in normal, non-pathological tissues            \u003ca rel=\"nofollow\"\u003e             PMID:                        17981779            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The spatiotemporal expression pattern of EpCAM changes during nephrogenesis            \u003ca rel=\"nofollow\"\u003e             PMID:                        18025791            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest that EpCAM is involved in signal transduction triggering several intracellular signalling pathways using tumor cell lines in colorectal and lung cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19002182            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM(+) cells isolated from injured liver proliferate to form colonies in vitro, and the clonally expanded cells differentiate into hepatocytes and cholangiocytes, suggesting that the oval cell fraction contains potential HSCs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19429791            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of EpCAM and DLK1 suggests the developmental pathways of mouse liver progenitors            \u003ca rel=\"nofollow\"\u003e             PMID:                        19527784            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43999205949665,"sku":"BLC-07570P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-MP007717MOf1-SDS.jpg?v=1690518354"},{"product_id":"recombinant-human-n-myc-proto-oncogene-protein-mycn-protein-his-blc-07871p","title":"Recombinant Human N-Myc Proto-Oncogene Protein (MYCN) Protein (His)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human N-Myc Proto-Oncogene Protein (MYCN) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P04198          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYCN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBaculovirus\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-6His\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1-464aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFull Length\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e50.6 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCancer\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBriefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg\/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C\/-80°C. The default final concentration of glycerol is 50%.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePositively regulates the transcription of MYCNOS in neuroblastoma cells.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7559           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            164280           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4613           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000281043           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30451831            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            This suggested that NMyc regulated survival and growth of CHP134 and BE2C neuroblastoma cells, potentially through Wnt\/betacatenin signaling. Furthermore, associated proteins, NMyc and STAT interactor and dickkopf Wnt signaling pathway inhibitor 1, were demonstrated to be involved in this regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749516            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this report, we present a case with Feingold Syndrome having a novel mutation in MYCN gene and discuss genetic counselling and prenatal diagnosis due to pregnancy of the patient's mother.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30204967            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results demonstrated that MYCN expression was downregulated in cholangiocarcinoma (CCA) through a mechanism involving miR-5095 binding its 3'UTR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29620172            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN levels are regulated transcriptionally by MYCNOS-01 (an alternative transcript of MYCNOS) in rhabdomyosarcoma and neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29466962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a MycN\/CIP2A-mediated cell-fate bias may reflect a possible mechanism underlying early priming of some aggressive forms of neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30021854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD133 expression and MYCN amplification induce chemoresistance and reduce average survival time in pediatric neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29322842            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that inter-play between MYCN and the highly tumorigenic proteins which are upregulated in the malignant IMR-32 neuroblastoma cells may be fueling their aggressive behavior.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29328367            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results suggest that MYCN serves as a prognostic biomarker and therapeutic target of ACR for liver cancer stem cell in de novo Hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29686061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Alternative nonhomologous DNA end-joining pathway proteins as components of MYCN oncogenic activity in human neural crest stem cell differentiation have been revealed in the process of neuroblastoma initiation in mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29238067            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TrkA expression is one of the most powerful predictor of good prognosis in neuroblastoma and is associated with younger age, lower stage, and absence of MYCN amplification            \u003ca rel=\"nofollow\"\u003e             PMID:                        29018959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of MYCN promoted cell proliferation, and induced erythroid differentiation block and apoptosis resistance to cytotoxic agent.  Knockdown of MYCN inhibited the expression of EZH2, and then activated p21 expression through removal of H3K27me3 at the p21 promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29022893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MAX to MYCN ratio that can account for tumour progression and clinical outcome in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29408445            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN expression is regulated by ZAR1 in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28791558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The target of miR-29b was predicted using miRanda, TargetScan and PicTar sofeware and authors also found MYCN was a direct target of miR-29b in glioma cells and miR-29b inhibited the proliferation of glioma cells via MYCN dependent way.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28423357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            eEF2K protects MYCN overexpressing NB cells from ND in vitro and in vivo, highlighting this kinase as a critical mediator of the adaptive response of MYCN amplified NB cells to metabolic stress.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574509            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Among 30 samples of brain tumor, 14 cases revealed MYCN amplification. High-protein expression of MYCN was also observed in 43.3% of patients. There was a significant correlation between MYCN gene amplification and protein expression, interestingly five case showed discrepancy between the gene amplification and protein expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28453467            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PRMT1 has a role in regulating MYCN in neuroblastoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27571165            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            N-myc levels appear to be modulated by the antagonistic interactions of both miR-17, as a negative regulator, and HuD, as a positive regulator in N-myc-amplified neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28560387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We also propose a model for the stabilization mechanism in which binding to Aurora-A alters how N-Myc interacts with SCF(FbxW7) to disfavor the generation of Lys48-linked polyubiquitin chains            \u003ca rel=\"nofollow\"\u003e             PMID:                        27837025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study provides a novel insight for miR-221 in the control of neuroblastoma cell proliferation and tumorigenesis, suggesting potentials of miR-221 as a prognosis marker and therapeutic target for patients with MYCN overexpressing neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28003306            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            N-MYC is in the downstream-regulated gene family in reprogramming cancer metabolism under hypoxia [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27447861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNHG1 is up-regulated by MYCN amplification and could be a potential prognostic biomarker for high-risk neuroblastoma intervention.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27517149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN expression is a marker indicative of likely clinical sensitivity to mTOR inhibition in neuroblastoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27438153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that MYCN and LSD1 co-localize at NDRG1 promoter and repress its expression in neuroblastoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27894074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate cross-talks between MYCN and beta-catenin signalling, which repress normal beta-catenin mediated transcriptional regulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27531891            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that transcription factor activating enhancer binding protein-4 (TFAP4) is a direct transcriptional target of MYCN in neuroblastoma and that high levels of this transcription factor are associated with poor clinical outcome in this disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27448979            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data extend knowledge on roles of MCPIP1 in our model and link the protein to regulation of expression and stability of MYCN through decrease of signaling via Akt\/mTOR pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27935099            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that MYCN and its regulated microRNAs acted together to repress the tumor suppressor genes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27167114            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Common genetic variation predisposes to different neuroblastoma genotypes, including the likelihood of somatic MYCN-amplification. [meta-analysis]            \u003ca rel=\"nofollow\"\u003e             PMID:                        29117357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results establish evidence that high MYCN amplification can be present in retinoblastoma with or without coding sequence mutations in the RB1 gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28211617            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study conducted metabolic profiling of pre-malignant sympathetic ganglia and tumors derived from the TH-MYCN mouse model of neuroblastoma, that overexpresses human MYCN and compared to non-malignant ganglia from wildtype littermates. These results identify enhanced glutathione biosynthesis as a selective metabolic adaptation required for initiation of MYCN-driven neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26996379            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many prognostic signatures for neuroblastoma are confounded by MYCN amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27599694            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increasing MYCN copy number is associated with an increasingly higher rate of unfavorable clinical\/biological features, with 11q aberration being an exception. Patients with MYCN gain appear to have inferior outcomes, especially in otherwise more favorable groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28696504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-21 enhances chemo-resistance in tongue cancer cells via directly targeting CADM1, and an inverse correlation between miR-21 and CADM1 expression in vivo. MiR-21 overexpression is attributed to MYCN-mediated transcriptional regulation, which is also predictive for a worse prognosis in tongue cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27055844            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LMO1 is an important oncogene that promotes neuroblastoma initiation, progression, and widespread metastatic dissemination.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867147            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results identify DOT1L as a novel cofactor in N-Myc-mediated transcriptional activation of target genes and neuroblastoma oncogenesis. Furthermore, they characterize DOT1L inhibitors as novel anticancer agents against MYCN-amplified neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28209620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CCCTC-binding factor (CTCF) targets the binding sites within MYCN promoter to facilitate its expression in neuroblastoma (NB) cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26549029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PAX3-FOXO1 collaborates with MYCN during early rhabdomyosarcoma (RMS) tumourigenesis to dysregulate proliferation and inhibit myogenic differentiation and cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28138962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings reveal a PLK1-Fbw7-Myc signaling circuit that underlies tumorigenesis and validate PLK1 inhibitors, alone or with Bcl2 antagonists, as potential effective therapeutics for MYC-overexpressing cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27773673            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that N-Myc overexpression leads to the development of poorly differentiated, invasive prostate cancer that is molecularly similar to human NEPC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27728805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Rac activity may be an important determinant of metastatic capability in subsets of neuroblastoma cells lacking MYCN amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27224546            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN Gene Amplification is associated with Neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27513929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN overexpression combined with activated anaplastic lymphoma kinase (ALK) is sufficient to induce neuroblastoma (NB) in mouse sympathoadrenal cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27707976            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYCN amplification can be heterogeneous between tumor sites, during tumor progression or following treatment, challenging the notion that MYCN copy number does not change for a particular neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27465929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High MycN expression is associated with low radiosensitivity in neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27432152            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            applying loss-and-gain function analysis, we demonstrated that miR-34a directly targeted to MYCN to sensitize NSCLC cells to cisplatin. In addition, p53 was found to monitor the expression of miR-34a in NSCLC cells after cisplatin treatment. Therefore, the sensitivity of cisplatin in NSCLC cells was modulated via p53\/miR-34a\/MYCN axis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27836543            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data supports our hypothesis that a positive-feedback loop of sonic hedgehog signaling induced INSM1 through N-myc and INSM1 enhanced N-myc stability contributing to the transformation of human neuroblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26456864            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog (MYCN) was overexpressed in non-small cell lung cancer (NSCLC) tumor tissues and cell lines, suggesting that targeting MYCN might provide beneficial effects for the clinical therapy of NSCLC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27449038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            That initial decision to deny coverage could have had untoward health implications for this child, as the identification of constitutional MYCN duplication necessitated surveillance imaging for a number of pediatric malignancies associated with MYCN            \u003ca rel=\"nofollow\"\u003e             PMID:                        27794475            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43999237144801,"sku":"BLC-07871P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-BP015278HU-SDS.jpg?v=1690519335"},{"product_id":"recombinant-human-myc-proto-oncogene-protein-myc-protein-his-gst-blc-11200p","title":"Recombinant Human Myc Proto-Oncogene Protein (MYC) Protein (His-GST)","description":"\u003cmeta charset=\"utf-8\"\u003e\u003ch3\u003eProduct Overview\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Myc Proto-Oncogene Protein (MYC) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUniprotkb\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca rel=\"nofollow\" target=\"_blank\"\u003e           P01106          \u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Symbol\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMYC\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonyms\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAU016757; Avian myelocytomatosis viral oncogene homolog; bHLHe39; c Myc; Cellular myelocytomatosis oncogene; Class E basic helix-loop-helix protein 39; MGC105490; MRTL; Myc; Myc protein; Myc proto oncogene protein; Myc proto-oncogene protein; myc-related translation\/localization regulatory factor; MYC_HUMAN; Myc2; myca; MYCC; Myelocytomatosis oncogene a; Myelocytomatosis oncogene; Niard; Nird; oncogene c-Myc; Oncogene Myc; OTTHUMP00000158589; OTTHUMP00000227763; Proto-oncogene c-Myc; Protooncogene homologous to myelocytomatosis virus; RNCMYC; Transcription factor p64; Transcriptional regulator Myc-A; V-Myc avian myelocytomatosis viral oncogene homolog; v-myc myelocytomatosis viral oncogene homolog (avian); zc-myc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSpecies\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHomo sapiens (Human)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression System\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eE.coli\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eN-6His-GST\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Protein Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eExpression Range\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e169-439aa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Length\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePartial\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMol. Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e61.7 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eResearch Area\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEpigenetics And Nuclear Signaling\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eForm\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid or Lyophilized powder\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBuffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLiquid form: default storage buffer is Tris\/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris\/PBS-based buffer, 6% Trehalose, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e1. Store at -20°C\/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C\/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C\/-80°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eNotes\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTranscription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus, nucleoplasm. Nucleus, nucleolus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7553           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            113970           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4609           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000367207           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30226609            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            lncRNA THOR is up-regulated in retinoblastoma, and its over-expression significantly enhances the malignant phenotype transformation of retinoblastoma cells by up-regulating c-myc and TGF2BP1 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30119193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we demonstrate that neither MYC IHC nor MYC FISH alone is a sufficient screening mechanism for identification of the clinically relevant entities of HGBLwR or DEL            \u003ca rel=\"nofollow\"\u003e             PMID:                        28868942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Because RPL23 is encoded by a target gene of c-Myc, the RPL23\/Miz-1\/c-Myc regulatory circuit provides a feedback loop that links efficient RPL23 expression with c-Myc's function to suppress Miz-1-induced Cdk inhibitors and thereby leads to apoptotic resistance in higher-risk myelodysplastic syndrome patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28539603            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GATAD2B interacts with C-MYC to enhance KRAS driven tumor growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30013058            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            low expression of c-Myc protein predicts poor outcomes in patients with HCC with hepatectomy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29690860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Combined, these findings suggest that c-Myc could transcriptionally regulate TCRP1 in cell lines and clinical samples and identified the c-Myc-TCRP1 axis as a negative biomarker of prognosis in tongue and lung cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28623290            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Kazakh and Han patients with esophageal squamous cell carcinoma with Glut1 c-myc co-expression had poorer prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29629851            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC activation in papillary clear cell renal cell carcinoma leads to a worse prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28593993            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            could not find any relationship between Bcl-2, c-Myc and EBER-ISH positivity and the low\/high IPS groups in classical Hodgkin lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29708579            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fluorescence in situ hybridization studies (histologic sections) confirmed translocations of MYC (8q24), BCL2 (18q21) and BCL6 (3q27) in all patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30043475            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            topical mevastatin accelerates wound closure by promoting epithelialization via multiple mechanisms: modulation of GR ligands and induction of the long noncoding RNA Gas5, leading to c-Myc inhibition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CCND1 , C-MYC , and FGFR1 amplifications were observed in 34.28%, 28.57%, and 17.14% of the 35 samples (invasive ductal breast carcinoma).            \u003ca rel=\"nofollow\"\u003e             PMID:                        30119151            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that MYC induction of REV-ERBalpha is both persistent and recurrent across many inducible MYC model systems.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28332504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HUWE1 overexpression could functionally suppress prostate carcinoma development both in vitro and in vivo, possibly by inverse regulation of c-Myc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29966975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Menin functions as an oncogenic regulatory factor that is critical for MYC-mediated gene transcription.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28474697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Melatonin disturbs SUMOylation-mediated crosstalk between c-Myc and nestin via MT1 activation and promotes the sensitivity of paclitaxel in brain cancer stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29654697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FBP1 modulates the sensitivity of pancreatic cancer cells to BET inhibitors by decreasing the expression of c-Myc. These findings highlight FBP1 could be used as a therapeutic niche for patient-tailored therapies            \u003ca rel=\"nofollow\"\u003e             PMID:                        30201002            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR135a directly bound to UCA1 and the 3' untranslated region of cmyc, and UCA1 competed with cmyc for miR135a binding.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC directly regulates DANCR and plays important role in cancer cell proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29180471            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this review, we provide support to the hypothesis that the cooperation of c-Myc with transcriptional cofactors mediates c-Myc-induced cellular functions. We produce evidence that recently identified cofactors are involved in c-Myc control of survival mechanisms of cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        30261904            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            4-chlorobenzoyl berbamine (CBBM) inhibits the JAK2\/STAT3 pathway, leading to reduced c-Myc transcription. Collectively, these findings suggest that CBBM could be a promising lead compound for treatment of c-Myc-driven diffuse large B cell lymphoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30099568            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results revealed that C-MYC protein is highly expressed in colon cancer tissues, mainly in the cell nucleus and was identified as a direct target for mir-184. C-MYC appeared to participate in cell cycle regulation and malignant transformation to colon cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28782841            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MACC1 and c-Myc are highly expressed in serum and tumor tissues of EC patients. Both are correlated with TNM stage, primary infiltration, and lymph node or distal metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29984790            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study provides an interesting example using chemical biological approaches for determining distinct biological consequences from inhibiting vs. activating an E3 ubiquitin ligase and suggests a potential broad therapeutic strategy for targeting c-MYC in cancer treatment by pharmacologically modulating cIAP1 E3 ligase activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30181285            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The data demonstrated that 10058F4, a cMyc inhibitor, increased the growth inhibition, G0\/G1 phase arrest and apoptosis of the NALM6 and CEM cells as induced by dexamethasone (DXM), a type of GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749488            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-MYC\/BCL2 protein co-expression is associated with non-germinal center B-cell in Diffuse Large B-Cell Lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29801406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-Myc was capable of upregulating HP1gamma by directly binding to the E-box element in the first intron of HP1gamma gene, and the upregulated HP1gamma, in turn, repressed the expression of miR-451a by enhancing H3K9 methylation at the promoter region of miR-451a.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28967902            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A subset of pancreatic acinar cell carcinomas shows c-MYC alterations including gene amplification and chromosome 8 polysomy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29721608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression and Clinical Significance of LC-3 and P62 in Non-small Cell Lung Cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29945702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of the current study demonstrate presence of the IDH1 R132H mutation in primary human glioblastoma cell lines with upregulated HIF-1alpha expression, downregulating c-MYC activity and resulting in a consequential decrease in miR-20a, which is responsible for cell proliferation and resistance to standard temozolomide treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29625108            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a novel signal circuit of Stat3\/Oct-4\/c-Myc was identified for regulating stemness-mediated Doxorubicin resistance in triple-negative breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29750424            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC amplification and MYC overexpression occurred almost exclusively in secondary cutaneous angiosarcoma in our series.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29135507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High c-myc expression is associated with the development of prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29554906            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circular RNA hsa_circRNA_103809 promotes lung cancer progression via facilitating ZNF121-dependent MYC expression by sequestering miR-4302.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29698681            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors conclude that quantitative measurements of intratumor heterogeneity by multiplex FISH, detection of MYC amplification and TP53 mutation could augment prognostication in breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29181861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCYT1A was upregulated by MYC, which resulted in the induction of aberrant choline metabolism and the inhibition of B-lymphoma cell necroptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28686226            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cryptic t(3;8)(q27;q24) and\/or MYC-BCL6 linkage associated with MYC expression by immunohistochemistry is frequent in multiple-hit B-cell lymphomas.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28665415            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD30+ diffuse large B-cell lymphoma has characteristic clinicopathological features mutually exclusive with MYC gene rearrangement and negatively associated with BCL2 protein expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29666157            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High MYC amplification is associated with HER2 positive breast cancers in African American women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29523126            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest that MYC acts as a master coordinator that inversely modulates the impact of cell cycle and circadian clock on gene expression via its interaction with MIZ1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27339797            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In our study, the c-myc oncogene was amplified in 11.1% of BPH samples. Bivariate analysis failed to reveal any significant association between oncogene amplification and the clinicopathologic variables examined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29234244            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic variation at the 8q24.21 renal cancer susceptibility locus affects HIF1A and HIF1B binding to a MYC enhancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27774982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that miR-34a enhanced the sensitivity to cisplatin by upregulation of c-Myc and Bim pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29060932            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Luciferase reporter assay showed that c-Myc, an oncogene that regulating cell survival, angiogenesis and metastasis, was a direct target of miR-376a. Over-expression of miR-376a decreased the mRNA and protein levels of c-Myc in A549 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28741879            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present findings show that expression of c-MYC has prognostic value in squamous cell carcinoma of the tongue, and could be useful in choice of therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28393404            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Multivariable analysis indicated that IPI (P = 0.002), chemotherapy regimens (P = 0.017), and MYC gene rearrangements (P = 0.004) were independent adverse prognostic factors for all diffuse large B cell Lymphoma(DLBCL) patients in this study. Results demonstrated that the poor survival of DLBCL patients with HBV infection was closely involved in chemotherapy regimens, IPI, and MYC gene rearrangements            \u003ca rel=\"nofollow\"\u003e             PMID:                        29209623            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MYC extra copy in diffuse large B-cell lymphoma is an independent poor prognostic factor            \u003ca rel=\"nofollow\"\u003e             PMID:                        28776574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The c-Myc\/miR-200b\/PRDX2 loop regulates colorectal cancer (CRC) progression and its disruption enhances tumor metastasis and chemotherapeutic resistance in CRC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29258530            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20ug","offer_id":43999654543585,"sku":"BLC-11200P","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CSB-EP015270HU1-SDS.jpg?v=1690529943"}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/collections\/Protein_CD47_PDB_2JJS_912afe47-4156-4b67-952f-5e562281ddc4.png?v=1778547858","url":"https:\/\/www.betalifesci.com\/collections\/myc-protein-overview-applications-selection-guide.oembed","provider":"Beta LifeScience","version":"1.0","type":"link"}