Recombinant Mouse Myc Proto-Oncogene Protein (MYC) Protein (GST)

Name: Recombinant Mouse Myc Proto-Oncogene Protein (MYC) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02928P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Myc Proto-Oncogene Protein (MYC) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P01108
Target Symbol	MYC
Synonyms	Myc; Myc proto-oncogene protein; Proto-oncogene c-Myc; Transcription factor p64
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA
Expression Range	1-439aa
Protein Length	Full Length
Mol. Weight	76.0kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid 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.
Reconstitution	Briefly 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%.
Storage	1. 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.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Transcription 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.
Subcellular Location	Nucleus, nucleoplasm. Nucleus, nucleolus.
Database References	KEGG: mmu:17869 STRING: 10090.ENSMUSP00000022971 UniGene: PMID: 29249668 amino acid-controlled cMyc has an essential role in NK cell metabolism and function PMID: 29904050 Kidney specific MYC activation results in papillary clear cell renal cell carcinoma. PMID: 28593993 c-Myc is essential for tumor initiation, maintenance, and metastasis. PMID: 29440228 Genomic characterization of Emu-Myc mouse lymphomas identifies Bcor as a Myc cooperative tumor-suppressor gene. PMID: 28262675 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. PMID: 28148912 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. PMID: 29170413 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. PMID: 29396161 Myc is a component that links neuromesodermal progenitors maintenance and pre-somitic mesoderm maturation during the body axis elongation stages of mouse embryogenesis. PMID: 30061166 Myc potentiates the Wnt/beta-catenin signalling pathway, which cooperates with the transcriptional regulatory network in sustaining embryonic stem cell self-renewal. PMID: 27301576 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 PMID: 29342133 Conditional deletion of Myc in hyaloid vascular endothelial cells suppressed both proliferation and cell death. PMID: 29777010 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. PMID: 28159836 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. PMID: 28847964 High myc expression is associated with Intestinal Tumorigenesis. PMID: 29533773 results shed light on how overexpressed MYC alters the various phases of the RNAPII cycle and the resulting transcriptional response. PMID: 28904013 c-Myc overexpression stimulated proliferation and activation of renal fibroblasts by inducing integrin alphav-mediated TGF-beta signaling. PMID: 28483378 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. PMID: 27549025 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. PMID: 27752085 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. PMID: 28548937 this study demonstrates that miR-451 regulates T cell proliferative responses in part via a Myc-dependent mechanism PMID: 28378118 AKAP1 is a transcriptional target of Myc, and it supports mTOR pathway and the growth of cancer cells. PMID: 28569781 High c-myc expression is associated with gliomagenesis. PMID: 26993778 the role of phosphorylation on AID serine38 in AID activity at the Immunoglobulin switch region and off-target Myc gene, is reported. PMID: 29122947 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. PMID: 29074502 Results show Myc to be dispensable for sustained in vivo hepatocyte proliferation but necessary for maintaining normal lipid homeostasis. PMID: 27105497 Pin1 silencing in lymphomas retarded disease progression in mice, making Pin1 an attractive therapeutic target in Myc-driven tumors. PMID: 26943576 beta-catenin cooperates with the transcription factor Myc to activate the progenitor renewal program. PMID: 28993399 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. PMID: 28329683 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. PMID: 27926868 miR-17-92-dependent tuning of LKB1 levels regulates both the metabolic potential of Myc+ lymphomas and tumor growth in vivo. PMID: 27498867 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. PMID: 28989026 B-cell receptor controls fitness of MYC-driven lymphoma cells via GSK3beta inhibition PMID: 28562582 High Myc expression is associated with hepatocarcinogenesis. PMID: 28481866 Myc-high embryonic stem cells (ESCs) approach the naive pluripotency state, whereas Myc-low ESCs are closer to the differentiation-primed state. PMID: 28919206 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. PMID: 28504719 by controlling both nanodomain decompaction and PolII promoter escape Myc stands as a master regulator of transcriptome amplification during B cell activation. PMID: 28803781 these results indicate that PIAS1 is a positive regulator of MYC. PMID: 27239040 this study shows that that deletion of Sox2 increases the frequency of IgH:c-Myc translocations PMID: 28188246 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 PMID: 28530645 Data show that Emu-Myc mice lacking both p21 and PUMA developed lymphoma at a rate considerably longer latency than Emu-Myc;p53(+/-)mice. PMID: 26640149 CRY2 and FBXL3 cooperatively degrade c-MYC preventing the development of cancer. PMID: 27840026 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] PMID: 28652407 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. PMID: 28219903 MYC mediates cell cycle re-entry of Trp53-altered hepatocytes via AURKA binding. PMID: 27213815 Myc can substitute for Notch1 in leukemogenesis PMID: 27670423 our results show how MYC drives the production of specific eicosanoids critical for lung cancer cell survival and proliferation PMID: 27335109 Early generated B1 B cells with restricted BCRs become chronic lymphocytic leukemia with continued c-Myc and low Bmf expression PMID: 27899442 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). PMID: 28432125 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. PMID: 27301468

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.