Recombinant Human Epiregulin (Catalog # 1195-EP) stimulates proliferation in the Balb/3T3 mouse embryonic fibroblast cell line. The ED50 is 0.125-0.75 ng/mL.
1 μg/lane of Recombinant Human Epiregulin was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 5 kDa.
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. (1991) Proc. Natl. Acad. Sci. USA 88:415. The ED50 for this effect is 0.125-0.75 ng/mL.
Source
E. coli-derived human Epiregulin protein Val63-Leu108, with an N-terminal Met
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
5.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 1195-EP in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Epiregulin Protein
Epiregulin
ER
EREG
proepiregulin
Background
Epiregulin is a member of the EGF family of growth factors which includes, among others, epidermal growth factor (EGF), transforming growth factor (TGF)-alpha, amphiregulin (ARG), HB (heparin-binding)-EGF, betacellulin, and the various heregulins. All EGF family members are synthesized as transmembrane precursors and are converted to soluble forms by proteolytic cleavage. Epiregulin was originally purified from the mouse fibroblast-derived tumor cell line NIH3T3/T7 (1). The human epiregulin cDNA encodes a 169 amino acid (aa) residues transmembrane precursor with a 29 aa signal peptide, a 21 aa transmembrane domain and a 21 aa cytoplasmic domain. The putative soluble mature Epiregulin comprising the EGF-like domain (aa residues 64-104) is formed by proteolytic removal of the propeptide regions (2). There is 85% aa sequence homology between human and mouse epiregulins. Epiregulin is expressed primarily in the placenta and macrophages (3). High level expression has also been detected in various carcinomas. Epiregulin specifically binds EGFR (ErbB1) and ErbB4 but not ErbB2 and ErbB3. It activates the homodimers of both ErbB1 and ErbB4. In addition, epiregulin can also activate all possible heteromeric combinations of the four ErbB family members (4). Epiregulin stimulates the proliferation of fibroblasts, smooth muscle cells and hepatocytes. It has been shown to be an autocrine growth factor for epidermal keratinocytes as well as mesangial cells (5, 6). Epiregulin has also been shown to inhibit growth of several epithelial tumor cells. In addition, Epiregulin has been implicated in the implantation process during pregnancy (7).
Toyoda, H. et al. (1995) J. Biol. Chem. 270:7495.
Toyoda, H. et al. (1997) Biochem. J. 326:69.
Komurasaki, T. et al. (1997) Oncogene 15:2841.
Shelly, M. et al. (1998) J. Biol. Chem. 273:10496.
Shirakata, Y. et al. (2000) J. Biol. Chem. 275:5748.
Mishre, R. et al. (2002) Am. J. Physiol. Renal. Physiol. 283:F1151.
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