Recombinant Human Proepiregulin (EREG), Active

Beta LifeScience SKU/CAT #: BLC-05975P

Recombinant Human Proepiregulin (EREG), Active

Beta LifeScience SKU/CAT #: BLC-05975P
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Product Overview

Description Recombinant Human Proepiregulin (EREG), Active is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 97% as determined by SDS-PAGE and HPLC.
Endotoxin Less than 1.0 EU/μg as determined by LAL method.
Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 2 ng/ml, corresponding to a specific activity of >5.0x10 5 IU/mg.
Uniprotkb O14944
Target Symbol EREG
Synonyms Epiregulin; EPR; ER ; Ereg; EREG_HUMAN; Proepiregulin
Species Homo sapiens (Human)
Expression System E.Coli
Tag Tag-Free
Complete Sequence VAQVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL
Expression Range 60-108aa
Protein Length Partial
Mol. Weight 5.6 kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer 0.2 μm filtered PBS, pH 7.4, lyophilized
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.

Target Details

Target Function Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation. Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation.
Subcellular Location [Epiregulin]: Secreted, extracellular space.; [Proepiregulin]: Cell membrane; Single-pass type I membrane protein.
Database References

HGNC: 3443

OMIM: 602061

KEGG: hsa:2069

STRING: 9606.ENSP00000244869

UniGene: PMID: 29091309

  • we showed that epidermal growth factor receptors (EGFR) were constitutively activated in metastatic lung subtypes of salivary adenoid cystic carcinoma cells, and that this activation was induced by autocrine expression of epiregulin PMID: 26958807
  • Study shows how the EGFR ligands epiregulin (EREG) and epigen (EPGN) stabilize different dimeric conformations of the EGFR extracellular region. Results reveal how responses to different EGFR ligands are defined by receptor dimerization strength and signaling dynamics. These findings have broad implications for understanding receptor tyrosine kinase (RTK) signaling specificity. PMID: 28988771
  • EREG and MMP-1 were found to be elevated in nasal polyp and uncinate tissues in patients with Chronic rhinosinusitis with nasal polyps. PMID: 28398769
  • upregulation of EREG expression through promoter demethylation might be an important means of activating the EGFR pathway during the genesis of colorectal adenocarcinoma (CRC) and potentially other cancers. PMID: 27270421
  • EREG and AREG are strongly regulated by methylation, and their expression is associated with CIMP status and primary tumour site. PMID: 27272216
  • three-dimensional structure of the EPR antibody (the 9E5(Fab) fragment) in the presence and absence of EPR PMID: 26627827
  • Together, these studies lead to identification of a novel pathway involving EREG and MMP-1 that contributes to the formation of early stage breast cancer PMID: 26215578
  • These results suggested that EREG is one of the molecules involved in glioma malignancy PMID: 24470554
  • Data indicate that the effects of epiregulin (EREG) and V-ATPase (TCIRG1) single nucleotide polymorphism (SNP) on pulmonary tuberculosis susceptibility, to the extent that they exist, are dependent on gene-gene interactions in West African populations. PMID: 24898387
  • Patients homozygous for the minor allele A of EREG rs12641042 had a significantly higher 3-year survival rate than patients with allele C (HR 0.48; P=0.034), but significance was lost in multivariable analysis PMID: 25203737
  • Epiregulin is a transcriptional target of TSC2 (tuberin). PMID: 24748662
  • Epiregulin promotes the proliferation of liver progenitor cells and DNA synthesis by hepatocytes and is upregulated in the serum of patients with liver injury. PMID: 24812054
  • Plasma HGF and EREG levels are associated with resistance to treatment with anti-EGFR antibodies in KRAS wild-type patients with metastatic colorectal cancer. PMID: 24800946
  • Data suggest that EREG (epiregulin), AREG (amphiregulin), and BTC (betacellulin) induced prostaglandin E2 production by induction of COX-2 (prostaglandin-endoperoxide synthase 2) through MAP kinase signaling in granulosa cells. PMID: 24092824
  • In pre-treated K-ras wild-type status colorectal cancer, patients with high EREG gene expression appear to benefit more from cetuximab therapy compared with low expression. PMID: 24335920
  • EREG may contribute to glioma progression under the control of IRE1a. PMID: 24330607
  • keratinocyte hyperproliferation in cholesteatoma is promoted through overexpression of epiregulin by subepithelial fibroblasts via epithelial-mesenchymal interactions, which may play a crucial role in the pathogenesis of middle ear cholesteatoma PMID: 23826119
  • Depletion of Epiregulin with shRNA inhibited SCAP proliferation. PMID: 23829318
  • Data indicate that epiregulin (EREG) expression significantly correlated with KRAS expression or KRAS copy number in KRAS-mutant non-small-cell lung cancer (NSCLC) cell lines. PMID: 22964644
  • EREG-AREG and NRG1, which are members of the epidermal growth factor (EGF) family, seem to modulate Bhecet's Disease susceptibility through main effects and gene-gene interactions PMID: 23625463
  • we did not find a correlation between the presence of a K-ras mutation and the presence of Epiregulin and Amphiregulin in colon cancer tissue. PMID: 23885463
  • Apical mistrafficking of EREG crystallizes an apical EGFR signaling complex that may be uncoupled from basolateral regulatory restraints leading to cell transformation. PMID: 23671122
  • FBXL11 inhibited osteo/dentinogenic differentiation potential in MSC cells by associating with BCOR, then increasing histone K4/36 methylation in Epiregulin promoter to repress Epiregulin transcription. PMID: 23074094
  • EREG gene expression was low in 7 out of 11 gastric cancer cells and this downregulation was mediated by aberrant CpG methylation of the EREG promoter. PMID: 22508389
  • Epiregulin (EREG) variation is associated with susceptibility to tuberculosis. PMID: 22170233
  • Data suggest that expression status of AR and EPI mRNAs might be evaluated as dynamic predictors of response in KRAS WT patients receiving any cetuximab-based therapy. PMID: 21161326
  • It is suggested that follow-up of the expression of Ep can serve as a reliable early indication of the development of ovarian cancer. PMID: 21769422
  • Blockade of epiregulin reduced the growth of hTERT-BJ cells and colony formation of hTERT-transformed fibroblasts. Moreover, inhibition of epiregulin function in immortal hTERT-BJ cells triggered a senescence program. PMID: 12702554
  • Epiregulin might be a more important tumor growth regulator of malignant fibrous histiocytoma through autocrine or paracrine pathways, when compared with betacellulin. PMID: 15274392
  • upregulation of the epiregulin and amphiregulin expression is part of the signal transduction pathway which leads to ovulation and luteinization in the human ovary PMID: 15474502
  • findings demonstrated that PGE2 may mimic LH action at least in part by the activation of amphiregulin and epiregulin biosynthesis in human granulosa cells PMID: 16888076
  • epiregulin, COX2, and MMP1 and 2 collectively facilitate the assembly of new tumour blood vessels, the release of tumour cells into the circulation, and the breaching of lung capillaries by circulating tumour cells to seed pulmonary metastasis PMID: 17429393
  • 1st report of EREG expression in breast cancer (45.5% of breast cancers studied). It is preferentially expressed in breast tumors co-expressing HER2/HER4. PMID: 17962208
  • Epiregulin played an autocrine role in the proliferation of corneal epithelial cells presumably through cross-induction with other EGF family members. PMID: 18079685
  • hamartomatous TSC skin tumors are induced by paracrine factors released by two-hit cells in the dermis, and proliferation with mTOR activation of the overlying epidermis is an effect of epiregulin PMID: 18292222
  • Increased epiregulin is associated with oral squamous cell carcinomas PMID: 18497965
  • Epiregulin has a protective effect against apoptosis in the human corpus luteum. PMID: 18835871
  • The regulatory mechanism of epiregulin expression in Ki-ras-transformed 267B1 prostate epithelial cells was studied. PMID: 18948081
  • Epiregulin expression correlates with advanced disease, is EGFR dependent, and confers invasive properties on non-small cell lung cancer cells. PMID: 19138957
  • FAQs

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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.

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

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