Betacellulin (human, recombinant)

Betacellulin is a member of the EGF family of growth factors. It is composed of a signal peptide, an extracellular domain, which contains the EGF-like domain and a proteolytic cleavage site, a transmembrane domain, and a cytoplasmic domain. Betacellulin is ubiquitously expressed and undergoes shedding via cleavage by disintegrin and metalloproteinase domain-containing proteins (ADAMs) to release the soluble mature form. It acts as a ligand for homodimers of EGFR or HER4 and all possible heterodimers of EGFR, HER2, HER3, and HER4 to induce signaling through various pathways, including JNK, RAS/RAF/MEK/ERK, and Akt. Betacellulin has mitogenic activity toward pancreatic beta-cells in vitro and improves glucose tolerance in vivo. It is also involved in reproduction, mammary gland and neonatal gastrointestinal tract development, and adult neurogenesis. Intratumoral levels of betacellulin are increased in patients with lung adenocarcinoma. Cayman's Betacellulin (human, recombinant) protein can be used for cell-based assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of betacellulin (amino acids 32-111) fused to human IgG1 Fc at its C-terminus, consists of 321 amino acids, has a calculated molecular weight of 36 kDa, and a predicted N-terminus of Asp32 after signal peptide cleavage. The monomer migrates at approximately 43-46 kDa by SDS-PAGE under reducing conditions.. Protein function: Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. [The UniProt Consortium]