Measured by its ability to inhibit TGF-beta 1 activity on TF‑1 human erythroleukemic cells. The ED50 for this effect is 1680.39ng/ml in the presence of 1ng/ml of recombinant human TGF-beta 1. (Regularly tested)

Transforming growth factor-β (TGF-β) is an essential regulator in the processes of development, cell proliferation, and extracellular matrix deposition. TGF-β regulates cellular processes by binding to three high-affinity cell surface receptors: TGF-β receptor type I (TGF-β-RI), TGF-β receptor type II (TGF-β-RII), and TGF-ββ receptor type III (TGF-β-RIII). TGF-β RII is consists of a C-terminal protein kinase domain and an N-terminal ectodomain and belongs to transforming growth factor-beta (TGF-β) receptor subfamily. TGF-β RII has a protein kinase domain which can form a heterodimeric complex with another receptor protein and bind TGF-beta. This receptor/ligand complex phosphorylates protein will enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation.

Greater than 95% as determined by reducing SDS-PAGE. (QC verified)