mouse monoclonal IgG1; Thrombin R Antibody (ATAP2) is an IgG1 κ mouse monoclonal Thrombin R antibody (also designated thrombin receptor antibody, F2R antibody, coagulation factor II antibody, or PAR1 antibody) that detects the Thrombin R protein of mouse, rat and human origin by WB, IP, IF, IHC(P) and FCM. Thrombin R Antibody (ATAP2) is available as both the non-conjugated anti-Thrombin R antibody form, as well as multiple conjugated forms of anti-Thrombin R antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. Thrombin is a serine protease that is involved in platelet aggregation and blood coagulation. It is cleaved from its precursor, prothrombin, and converts fibrinogen to Fibrin in the final step of the clotting cascade. Thrombin mediates its regulatory effects by activating cell surface receptors. These receptors, including Thrombin R (also designated PAR-1, for protease-activated receptor-1), PAR-2 and PAR-3, are members of the G protein-coupled receptor family, and share a similar gene structure. Thrombin cleaves its receptor, releasing a 41 amino acid peptide that acts as a platelet agonist. Upon this activation by thrombin, the Thrombin Rs trigger an increase in cytosolic Ca(2+) concentration. Unactivated Thrombin R cycles between the cell surface and an intracellular pool, while activated Thrombin R internalizes rapidly and is degraded in the lysosomes. The human Thrombin R is also known to be regulated by Sp1 and Sp3 transcription factors.