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 0.3-1 ng/mL.
Source
E. coli-derived mouse Epiregulin protein Val56-Leu101, with an N-terminal Met
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
5.5 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 1068-EP/CF 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.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Epiregulin Protein, CF
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. They are all synthesized as transmembrane precursors and converted to soluble forms by proteolytic cleavage. Epiregulin was originally purified from the mouse fibroblast-derived tumor cell line NIH3T3/T7 (1). The mouse Epiregulin cDNA encodes for a transmembrane precursor of 162 amino acid in length, with the mature soluble form comprising residues 56 - 101 (2). The mode of action of Epiregulin is similar to other EGF family members in that it binds to and activates the tyrosine-kinase, ErbB-family receptors (ErbB1 through B4) (3). Although it stimulates phosphorylation of all four receptors, it appears to interact primarily with ErbB1 and ErbB4. Epiregulin has the broadest specificity of the EGF-like ligands but seems to preferentially activate heterodimeric receptor complexes (4). Epiregulin exhibits a variety of biological effects. It was originally shown to both inhibit growth of several epithelial tumor cells and stimulate growth of fibroblasts and other types of cells (1). Epiregulin expression is upregulated in a number of carcinoma cell lines. It has also been shown to be an autocrine growth factor in human epidermal keratinocytes (5). Epiregulin has also been shown to play a role in the early steps of pregnancy, regulating attachment of the blastocyst to the uterine epithelium during the implantation process (6).
Toyoda, H. et al. (1995) J. Biol. Chem. 270:7495.
Toyoda, H. et al. (1995) FEBS Lett. 377:403.
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.
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