Recombinant Human Proepiregulin (EREG), Active

Name: Recombinant Human Proepiregulin (EREG), Active
Brand: Beta LifeScience
SKU: BLC-05975P
Availability: InStock

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, 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 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: Hs.115263
Tissue Specificity	In normal adults, expressed predominantly in the placenta and peripheral blood leukocytes. High levels were detected in carcinomas of the bladder, lung, kidney and colon.

Gene Functions References

in Caco-2 CFTR-shRNA cells, the EGFR ligand EREG is overexpressed due to an active IL-1beta autocrine loop that indirectly activates EGFR, constituting new signaling effectors for the CFTR signaling pathway, downstream of CFTR, Cl(-) , and IL-1beta. 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

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.