Recombinant Human Transcriptional Regulator Erg (ERG) Protein (His-SUMO)

Name: Recombinant Human Transcriptional Regulator Erg (ERG) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08133P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Transcriptional Regulator Erg (ERG) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11308
Target Symbol	ERG
Synonyms	Avian erythroblastosis virus E-26 (v-ets) oncogene related; D030036I24Rik; Erg 3; Erg; ERG/EWS fusion gene; included; ERG/FUS fusion gene; included; ERG/TMPSSR2 fusion gene; included; ERG_HUMAN; ERG1; included; ERG2; included; ets related; ETS-related gene; KCNH2; Oncogene ERG; p55; TMPRSS2/ERG fusion; transcriptional regulator ERG (transforming protein ERG); Transcriptional regulator ERG; Transforming protein ERG; v ets avian erythroblastosis virus E26 oncogene; v ets avian erythroblastosis virus E26 oncogene related; v ets erythroblastosis virus E26 oncogene homolog; v ets erythroblastosis virus E26 oncogene like; v ets erythroblastosis virus E26 oncogene like isoform 2; v-ets erythroblastosis virus E26 oncogene; v-ets erythroblastosis virus E26 oncogene homolog (avian); V-ets erythroblastosis virus E26 oncogene like (Avian); isoform CRA_e
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MIQTVPDPAAHIKEALSVVSEDQSLFECAYGTPHLAKTEMTASSSSDYGQTSKMSPRVPQQDWLSQPPARVTIKMECNPSQVNGSRNSPDECSVAKGGKMVGSPDTVGMNYGSYMEEKHMPPPNMTTNERRVIVPADPTLWSTDHVRQWLEWAVKEYGLPDVNILLFQNIDGKELCKMTKDDFQRLTPSYNADILLSHLHYLRETPLPHLTSDDVDKALQNSPRLMHARNTGGAAFIFPNTSVYPEATQRITTRPDLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQLDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSSNSSCITWEGTNGEFKMTDPDEVARRWGERKSKPNMNYDKLSRALRYYYDKNIMTKVHGKRYAYKFDFHGIAQALQPHPPESSLYKYPSDLPYMGSYHAHPQKMNFVAPHPPALPVTSSSFFAAPNPYWNSPTGGIYPNTRLPTSHMPSHLGTYY
Expression Range	1-486aa
Protein Length	Full Length
Mol. Weight	70.6kDa
Research Area	Transcription
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	Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure.
Subcellular Location	Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Families	ETS family
Database References	HGNC: 3446 OMIM: 165080 KEGG: hsa:2078 STRING: 9606.ENSP00000381891 UniGene: PMID: 28695891 Nine primary prostate cancers that developed metachronous bone metastasis samples showed TMPRSS2-ERG fusions, which were associated with increased ERG expression at immunohistochemistry. mTOR pathway activation was documented in 6 patients PMID: 30190183 Data indicate a significant prognostic role for assessing transcriptional regulator ERG (ERG) and phosphatase and tensin homolog protein (PTEN) in men with prostate cancer. PMID: 30101374 There was no statistically significant difference in the expression of the ERG between patients and controls. Also, no correlation was detected between the expression of this gene and age of onset, disease duration and Expanded Disability Status Scale. PMID: 29488813 Here, the authors show that ERG, through its physical interaction with androgen receptor, induces AR aggregation and endoplasmic reticulum stress in the prostate glands of ERG transgenic mice. PMID: 28439080 Our results suggested that reduced expression of miR-1271 may be involved in the ERG expression and that miR-1271 could be a therapeutic target for ERG-positive prostate cancer patients PMID: 28551819 Evaluating the association between ERG expression and pathologic factors. PMID: 29948147 despite of their well-known adverse role in prognosis of AML, neither BAALC nor ERG expression levels at diagnosis had effect on survival of AML patients who underwent allo-HSCT. PMID: 29696374 ERG expression is lost in liver endothelial cells from cirrhotic patients with fibrosis related to alcoholic liver disease or primary biliary cirrhosis and inversely correlates with increased markers of endothelial-to-mesenchymal transition. PMID: 29026072 ERG expression is of limited prognostic value in acute myeloid leukemia. PMID: 27935581 Our findings indicate that TGF-beta signaling is a major determinant of EMT in T/E overexpressing LNCaP cells. PMID: 28445989 Findings reveal that PCa-associated ERG can interact and co-occupy with BRD4 in the genome, and suggest this druggable interaction is critical for ERG-mediated cell invasion and PCa progression. PMID: 27223260 this work provides novel insights in the regulation of ERG protein stability in prostate cancer PMID: 27626314 Study reveals that miR-200b/a/429 is an ERG target gene, which implicates an important role in TMPRSS2/ERG-dependent PCa development. PMID: 27191272 ERG and SOX9 are potential biomarkers for prediction of response to docetaxel treatment in metastatic castration-resistant prostate cancer patients. PMID: 27863438 A potential novel function of TMPRSS2-ERG as a major regulator of IGF1R gene expression. PMID: 27285981 Study shows that T2E fusion transcripts are associated with higher levels of AMACR mRNA in patients with atypical small acinar proliferation (ASAP) which represents an indicator of risk for prostate cancer in patients with ASAP. PMID: 29277318 TMPRSS2-ERG may have a role in progression of prostate neoplasms and in alteration of the metabolic profile PMID: 27276682 Detection of TMPRSS2-ERG in blood from Metastatic Resistant Prostate Cancer patients predicts resistance to docetaxel and it may be useful to select treatment and to avoid possible toxicities in refractory patients.TMPRSS2-ERG-positive patients had more adverse prognostic factors compared with TMPRSS2-ERG-negative. PMID: 26948395 Meta-analysis showed the prevalence of TMPRSS2:ERG fusions in prostate cancer to be highest in men of European descent (49%), followed by Asians (27%) and then African (25%) descent. PMID: 28633309 Data show that tumors displaying TMPRSS2-ERG fusions that retained interstitial genes were less likely to be associated with biochemical recurrence PMID: 29127096 ERG, FLI1, TAL1, and RUNX1 bind at all AML1-ETO-occupied regulatory regions, including those of the AML1-ETO gene itself, suggesting their involvement in regulating AML1-ETO expression levels. PMID: 27851970 four oncogenic ETS (ERG, ETV1, ETV4, and ETV5), and no other ETS, interact with the Ewing's sarcoma breakpoint protein, EWS. PMID: 27783944 We demonstrate a role for inflammation-induced oxidative stress in the formation of DNA breaks leading to recurrent TMPRSS2-ERG gene fusions. The transcriptional status and epigenetic features of the target genes influence this effect. PMID: 27926866 ERG signaling in prostate cancer is driven through PRMT5-dependent methylation of the androgen receptor. PMID: 27183006 NOTCH pathway inhibition antagonizes the growth and invasion of transmembrane protease serine 2 (TMPRSS2)-transforming protein ERG (ERG) (T2E) -positive prostate cancer cells. PMID: 28783165 findings have identified critical molecular mechanisms involving ERK-mediated ERG activation that could be exploited for therapeutic intervention in ERG-positive prostate cancers. PMID: 28887309 Detection of Gene Rearrangements in Circulating Tumor Cells: Examples of ALK-, ROS1-, RET-Rearrangements in Non-Small-Cell Lung Cancer and ERG-Rearrangements in Prostate Cancer.( PMID: 28560674 The TMPRSS2-ERG gene fusion is the most frequently observed genetic aberration in Prostate cancer. PMID: 28845585 Loss of ERG is associated with prostate tumors. PMID: 28186998 Data show that homogeneous ERG positivity is very rare in prostate cancer, especially in elderly patients. However, development of subpopulations with ERG fusions may be a much more frequent event in ERG negative cancer foci as previously believed. PMID: 27530104 Genome-wide gene expression profiling identified a network of VEGF-responsive and ERG-dependent genes. PMID: 28536097 ERG deletion is associated with acute lymphoblastic leukemia. PMID: 27776115 Study provide evidence that PTEN deletion and TMPRSS2-ERG gene fusion were mutually exclusive in patients with prostate neoplasm. TMPRSS2-ERG gene fusion was rare compared to peripheral zone tumors and to PTEN inactivation in T1a transition zone tumors. PMID: 27500376 ERG rearrangement, but not PTEN loss, is present in a minority of potential neoplastic precursor lesions in the prostate. PMID: 27189342 Patients with Prostate cancer had significantly higher levels of the prostate cancer-associated gene ERG in post-digital rectal examination urine extracellular vesicles. Continued analysis of urine EVs offers the potential discovery of novel biomarkers for pre-biopsy Prostate cancer detection. PMID: 28419548 loss of ERG and FLI1 might contribute to the pathogenesis of vascular lung complications through the induction of inflammation. PMID: 28248553 Neither the expression of aberrant proteins from internally deleted allele nor the reduced expression of wild type ERG seem to provide a plausible explanation of the specific biology of ERG -related leukemia subgroup. PMID: 27494621 Our results suggest that the immune response may differ between ERG negative and ERG positive prostatic carcinomas PMID: 28547958 identified five phosphorylated serines on endogenous ERG in T-ALL and AML cells. PMID: 27055868 miR-204 upregulates androgen receptor (AR ) and downregulates TMPRSS2/ERG through direct regulation of their promoter methylation and set of transcription factors during AR cancer-related reprogramming. PMID: 28050800 differential expression of TMPRSS2:ERG in urine exosomes in prostate cancer and controls PMID: 27144529 SPINK1 and ERG expressions are exclusive events in PCA. PMID: 27738792 This study focused on the clinical application value of ERG methylation level in blood of pregnant women as a biomarker in Down's syndrome. PMID: 28111453 ETV6 and IKZF1 are transcriptional regulators not just of ERG, but also of a number of genes regulated by a densely interconnected network of seven transcription factors. PMID: 27604872 Among 98 selected prostate carcinoma biopsies, 57 showed positive and 41 negative ERG staining. PMID: 28384107 The present study established evidence for the first two common PrCa risk variants differentially associated with TMPRSS2:ERG fusion status. TMPRSS2:ERG phenotyping of larger studies is required to determine comprehensive sets of variants with subtype-specific roles in prostate cancer. PMID: 27798103 ERG is recruited to mRNAs via interaction with the RNA-binding protein RBPMS, and it promotes mRNA decay by binding CNOT2, a component of the CCR4-NOT deadenylation complex. PMID: 27273514 Concurrent nuclear ERG and MYC protein overexpression is common in prostate cancer and defines a subset of locally advanced tumors. PMID: 27159573 Studies indicate that TMPRSS2-ERG fusion gene positive prostate cancers cells rewire intracellular signaling cascades and modulate gene and protein network. PMID: 28364793

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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.

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