Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
Protein C is a vitamin K-dependent plasma glycoprotein that is cleaved to its activated form by the thrombin-thrombomodulin complex. Protein C in its activated form contains a serine protease domain and functions in degradation of the activated forms of coagulation factors V and VIII. Protein C is a vitamin K-dependent serine protease produced in the liver and made up of 2 polypeptide chains. The 62 kDa proenzyme is activated by thrombin bound to an endothelial surface receptor and the active enzyme cleaves factor Va and VIIIa and thus inhibits blood coagulation. The molecular weight of the active enzyme is 55 kDa and the normal concentrations in human plasma is approximately 1-3 ng/mL because of the very fast turnover, the proenzyme concentration is approximately 3 µg/mL. Mutations in the Protein C gene have been associated with thrombophilia due to protein C deficiency, neonatal purpura fulminans, and recurrent venous thrombosis.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Activation peptide; Anticoagulant protein C; Autoprothrombin IIA; Blood coagulation factor XIV; prepro-protein C; protein C (inactivator of coagulation factors Va and VIIIa); type I protein C; Vitamin K-dependent protein C; Vitamin K-dependent protein C heavy chain; Vitamin K-dependent protein C light chain
Gene Aliases: APC; PC; PROC; PROC1; THPH3; THPH4
UniProt ID: (Human) P04070
Entrez Gene ID: (Human) 5624