EREG Human, HEK
HEK293 cells.
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Sterile filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.
EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
Epiregulin, a member of the EGF family, acts as a ligand for EGFR and most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors. Primarily found in the placenta, peripheral blood leukocytes, and certain carcinomas (bladder, lung, kidney, colon), Epiregulin promotes the proliferation of keratinocytes, hepatocytes, fibroblasts, and vascular smooth muscle cells while inhibiting growth in several tumor-derived epithelial cell lines. Synthesized initially as a 19.0 kDa glycosylated transmembrane precursor protein, human Epiregulin undergoes proteolytic cleavage to yield a mature secreted sequence of 6.0 kDa.
Recombinant Human EREG, produced in HEK293 cells, is a single, glycosylated polypeptide chain (amino acids 63-108a.a) with a molecular weight of 32.6 kDa. The protein comprises 289 amino acids. A 239 amino acid hIgG-His-Tag is fused to the C-terminus. Purification is achieved using proprietary chromatographic techniques.
Sterile filtered, colorless solution.
The EREG protein solution has a concentration of 0.25 mg/ml and contains 10% glycerol in Phosphate-Buffered Saline (pH 7.4).
For short-term storage (up to 2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity is determined to be greater than 90.0% using SDS-PAGE analysis.
Biological activity is assessed through a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 is determined to be less than or equal to 1 µg/ml.
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
HEK293 cells.
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
Product Science Overview
Epiregulin (EREG) is a member of the epidermal growth factor (EGF) family, which plays a crucial role in various cellular processes, including proliferation, differentiation, and survival. The recombinant form of human epiregulin, expressed in HEK293 cells, is widely used in research to study its biological functions and therapeutic potential.
Epiregulin is a protein encoded by the EREG gene, located on human chromosome 4q13 . The recombinant human epiregulin protein expressed in HEK293 cells typically contains the amino acid sequence Val63-Leu108 and is often tagged with an Fc region of human IgG1 for purification and detection purposes . The molecular weight of the recombinant protein is approximately 33.8 kDa, but due to glycosylation, it may migrate to 37-42 kDa in SDS-PAGE .
The recombinant human epiregulin protein is expressed in HEK293 cells, a human embryonic kidney cell line commonly used for protein production due to its high transfection efficiency and ability to perform post-translational modifications. The protein is purified to a high degree, with a purity of over 95% as determined by SDS-PAGE and HPLC . The endotoxin level is kept below 1 EU per μg of protein, ensuring its suitability for various biological assays .
Epiregulin functions as a ligand for the epidermal growth factor receptor (EGFR) and other members of the ERBB family of tyrosine-kinase receptors . It exhibits bifunctional regulatory properties, inhibiting the growth of several epithelial tumor cells while stimulating the growth of fibroblasts and other cell types . Epiregulin binds to the EGF receptors of epidermoid carcinoma A431 cells more weakly than EGF but is more potent as a mitogen for rat primary hepatocytes and Balb/c 3T3 A31 fibroblasts .
The mechanism of action of epiregulin involves its interaction with EGFR, leading to receptor dimerization and autophosphorylation . This activation triggers downstream signaling pathways, including the RTK signaling, Fc-epsilon receptor signaling, and neurotrophin signaling pathways . These pathways regulate various cellular processes, such as muscle cell differentiation and proliferation .
Recombinant human epiregulin is used in various research applications, including cell proliferation assays, receptor binding studies, and signaling pathway analyses. It is particularly valuable in cancer research, where it helps to elucidate the role of EGFR signaling in tumor growth and progression .
