Recombinant Human Thrombospond

Thrombospondin-1 (TSP1) is a member of the Thrombospondin family and is encoded by the gene THBS1 which is a subunit of a disulfide-linked homotrimeric protein. Thrombospondin-1 is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Thrombospondin-1 can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. TSP1 has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. TSP1 has been shown to be a natural inhibitor of neovascularization and tumorigenesis in healthy tissue. TSP1 interacts with no less than 12 cell adhesion receptors, including CD36, av integrins, b1 integrins, syndecan, and integrin-associated protein (IAP or CD47). It also interacts with various proteases involved in angiogenesis, including plasminogen, matrix metalloproteinase, thrombin, cathepsin, and elastase. Positive and negative modulation of endothelial cell adhesion, motility, and growth are attributed to TSP1. Recently, thrombospondin-1 was found to bind to the reelin receptors, ApoER2 and VLDLR, in so doing affecting neuronal migration in the rostral migratory stream.

SDS