Epiregulin (Protein|Antibody|cDNA Clone|ELISA Kit)

All Epiregulin reagents are produced in house and quality controlled, including 26 Epiregulin Gene, 2 Epiregulin Lysate, 2 Epiregulin Protein, 2 Epiregulin qPCR. All Epiregulin reagents are ready to use.

Recombinant Epiregulin proteins are expressed by HEK293 Cells with fusion tags as N-human IgG1-Fc.

EpiregulincDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each Epiregulin of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.

Epiregulin Protein (2)


Epiregulin Protein, Human, Recombinant (Fc Tag)


Expression host: HEK293 Cells

Human Epiregulin/EREG Protein 9005

Epiregulin Protein, Mouse, Recombinant (Fc Tag)


Expression host: HEK293 Cells

Mouse Epiregulin/EREG Protein 11768

Epiregulin cDNA Clone (26)


Epiregulin qPCR Primer (2)

Epiregulin Lysate (2)

Epiregulin (EREG) is a member of the epidermal growth factor family. Epiregulin (EREG) can function as a ligand of EGFR (epidermal growth factor receptor), as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors. Epiregulin (EREG) exhibit bifunctional regulatory properties: it inhibit the growth of several epithelial tumor cells and stimulated the growth of fibroblasts and various other types of cells. Epiregulin (EREG) bound to the EGF receptors of epidermoid carcinoma A431 cells much more weakly than did EGF, but was nevertheless much more potent than EGF as a mitogen for rat primary hepatocytes and Balb/c 3T3 A31 fibroblasts. These findings suggest that epiregulin (EREG) plays important roles in regulating the growth of epithelial cells and fibroblasts by binding to receptors for EGF-related ligands. Epiregulin (EREG) is the broadest specificity EGF-like ligand so far characterized: not only does it stimulate homodimers of both ErbB-1 and ErbB-4, it also activates all possible heterodimeric ErbB complexes.