TGF-β1, Human

USA

-80°C

TGF-beta1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-beta1 superfamily that share a characteristic cystine knot structure. TGF-beta1, -2 and -3 are highly pleiotropic cytokines that act as cellular switches to regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-beta isoform has some non-redundant function; for TGF-beta1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-beta1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-beta RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-beta RI (also called activin receptor?like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.
Recombinant Human TGF-beta1 produced in CHO cells is a polypeptide chain containing 112 amino acids. A fully biologically active molecule, rhTGF-beta1 has a molecular mass of 12 kDa, analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.