Description |
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 callagen 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 inhibior of neovascularization and tumorigenesus 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, urokinase, matrix metalloproteinase, thrombin, cathepsin, and elastase. Positive and negative modulation of endothelial cell adhesion, motility, and growth are attibuted 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. Recombinant Human THBS1 is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. Recombinant Human THBS1 is Reactive with A4.1 anti-TSP mAb. |