thbs 1

Expression system: E. coli
Length: 19-350, Partial
Activity: Not Tested

Thrombospondin-1 (TSP-1) is a 150-180kDa calcium-sensitive protein that is secreted as a disulfide-linked homotrimer. TSP-1 regulates a wide range of cellular functions including their interactions with other cells and with the extracellular matrix (ECM). TSP-1 contains an N-terminal Laminin G-like globular domain, an extended central region with one vWFC domain, 3 TSP type 1domains, 2 EGF-like domains, and 8 TSP type3 domains, and a globular TSP C-terminal domain. Distinct regions of TSP-1 have been associated with binding to particular ECM or cellular molecules. TSP-1 counteracts the angiogenic, hypotensive, and antithrombotic effects of nitric oxide (NO). It binds and neutralizes VEGF, blocks VEGF R2 signaling on vascular endothelial cells(EC), and destabilizes adhesive contacts between EC. TSP-1 also plays an important role in wound repair and tissue fibrosis by binding latent TGF-beta and inducing release of the active cytokine from the latency associated peptide (LAP).

Cartilage Oligomeric Matrix Protein (COMP), also referred to as Thrombospondin-5, is a non-collagenous extracellular matrix (ECM) protein and belongs to the subgroup B of the thrombospondin protein family. This protein is expressed primarily in cartilage, ligament, and tendon, and binds to other ECM proteins such as collagen I, II and IX with high affinities depending on the divalent cations Zn2+ or Ni2+. COMP is a secreted glycoprotein that is important for growth plate organization and function. It is suggested to play a role in cell growth and development, and recent studies have revealed the possible mechanism that it protects cells against death by elevating members of the IAP (inhibitor of apoptosis protein) family of survival proteins. Mutations in COMP cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1), and up-regulated expression of COMP are observed in rheumatoid arthritis and certain carcinomas.