Recombinant Human Twisted Gastrulation (TSG) (carrier-free)
Description
Twisted gastrulation, or TSG, is a secreted glycoprotein bone morphogenetic protein, also known as BMP, antagonist. It was initially identified in Drosophila and modulates morphogenetic effects of the decapentaplegic (Dpp) morphogen. In vertebrate embryos, TSG controls the Dpp’s orthologs (BMP2 and 4). It is highly conserved, thus TSGs from different species are functionally equivalent. The activity of BMPs is controlled by the antagonists Noggin, Chordin, Chordin-like 1, Chordin-like 2, and TSG. BMP antagonists function through direct association with BMPs, inhibiting the binding of BMPs to their receptors. TSG strengthens the inhibitory complex formed by chording and BMPs. TSG also acts as a BMP agonist by promoting cleavage of chordin by tolloid-family proteinases. TSG is expressed by mouse thymocytes and up-regulated during the transition from the DN to the DP and from the DP to the CD4+ or CD8+ single-positives. TSG synergizes with chordin to block the BMP4-mediated inhibition of thymocyte proliferation and differentiation. BMP signaling and its regulation have direct effects on osteoclast differentiation and activities. TSG is a key modulator of BMP signaling, so it inhibits osteoclast differentiation. Also, TSG plays a critical role in the modulation of protective action of Bmp7 on podocytes. TSG exacerbates podocyte injuries, which is the first step in the progression of glomerulosclerosis.