Thrombin Receptor Antibodies

Thrombin is a coagulation protease produced at sites of vascular injury that activates platelets, endothelial cells, leukocytes and mesenchymal cells via cleavage of specific cell surface receptors known as proteinase activated receptors (PARs). A functional thrombin receptor from human platelets has been cloned and sequenced. It is a 66-kDa, single polypeptide chain that belongs to the cell surface G-protein-coupled receptor family, with seven transmembrane domains and an extracellular N terminus. The thrombin cleavage site is located in the N terminus between Arg41 and Ser42. Following cleavage by thrombin, activated receptors undergo desensitization and internalization but a fraction of them are recycled to the cell surface. The Thrombin Receptor is expressed on a variety of cells including platelets and endothelium. The receptor is a substrate of thrombin and has been shown to play a role in the activation of platelets.

Clone: SPAN 12 Isotype: IgG1 Mouse

The SPAN 12 antibody recognizes an epitope on the receptor that spans the thrombin cleavage site. It binds to intact receptors, but not to cleaved ones. SPAN 12 inhibits thrombin-induced receptor activation at reduced thrombin concentrations.

Clone: WEDE15 Isotype: IgG1 Mouse

The WEDE15 antibody recognizes an epitope on the receptor, distant from the N‑terminal thrombin cleavage site (WEDEE). It reacts with both intact and cleaved receptors.

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