epitope corresponding to amino acids 1-111 mapping at the N-terminus of Thrombin receptor of human origin
Modification Notes
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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Thrombin receptor of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-111 mapping at the N-terminus of Thrombin receptor of human origin
Tissue Specificity
epitope corresponding to amino acids 1-111 mapping at the N-terminus of Thrombin receptor of human origin