Neuregulin/Heregulin is a family of structurally-related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). To date, there are over 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms releases soluble growth factors. HRG1-β1 contains an Ig domain and an EGF-like domain; the latter is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding induces erb3 and erb4 heterodimerization with erb2, stimulating intrinsic kinase activity that leads to tyrosine phosphorylation. Although HRG1-β1's biological effects are still unclear, it has been found to promote motility and invasiveness of breast cancer cells, which may also involve up-regulation of expression and function of the autocrine motility-promoting factor (AMF). Recombinant Human Heregulinβ-1 (HRG1-B1) is a 7.5 kDa polypeptide consisting of only the EGF domain of heregulinβ-1 (65 amino acid residues).
Neuregulin1 (NRG1-β1), Neu differentiation factor (rat), HRG, HRG1-β1, Breast cancer cell differentiation factor p45, ARIA (Acetylcholine, Receptor Inducing Activity), glial growth factor
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE
≥ 98% by SDS-PAGE gel and HPLC analyses.
The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is ≤ 0.5 ng/ml, corresponding to a specific activity of ≥ 2 x 106 units/mg.
Calculated Molecular Weight:
Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug)
Not for human use.