![TGF-β1, Human TGF-β1, Human](/product/documents/down?doc_name=Z03411_Activity.jpg&file=scm_files/productFile_notes/2018/04/17/0e8e9fed46a2e86e61409bea2e538e30.jpg)
ED₅₀< 0.2ng/mL, measured in ability to inhibit the mouse IL-4-dependent proliferation of HT-2 cells.
TGF-β1, Human
TGF-β1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-β1 superfamily that share a characteristic cystine knot structure. TGF-β1, -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-β isoform has some non-redundant function; for TGF-β1, mice with targeted deletion show defects in hematopoiesis and endothelial differentiation and died of overwhelming inflammation. TGF-β1 signaling begins with high-affinity binding to a type II ser/thr kinase receptor termed TGF-β RII. This receptor then phosphorylates and activates a second ser/thr kinase receptor, TGF-β RI (also called activin receptor‑like kinase (ALK)-5), or alternatively, ALK-1. This complex phosphorylates and activates Smad proteins that regulate transcription.
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