|Other Names||Plasma kallikrein, Fletcher factor, Kininogenin, Plasma prekallikrein, Plasma kallikrein heavy chain, Plasma kallikrein light chain, KLKB1, KLK3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP14109b was selected from the C-term region of KLKB1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.|
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Plasma prekallikrein is a glycoprotein that participatesin the surface-dependent activation of blood coagulation,fibrinolysis, kinin generation and inflammation. It is synthesizedin the liver and secreted into the blood as a single polypeptidechain. Plasma prekallikrein is converted to plasma kallikrein byfactor XIIa by the cleavage of an internal Arg-Ile bond. Plasmakallikrein therefore is composed of a heavy chain and a light chainheld together by a disulphide bond. The heavy chain originatesfrom the amino-terminal end of the zymogen and contains 4 tandemrepeats of 90 or 91 amino acids. Each repeat harbors a novelstructure called the apple domain. The heavy chain is required forthe surface-dependent pro-coagulant activity of plasma kallikrein.The light chain contains the active site or catalytic domain of theenzyme and is homologous to the trypsin family of serine proteases.Plasma prekallikrein deficiency causes a prolonged activatedpartial thromboplastin time in patients.
MacKenzie, J.A., et al. Appl Physiol Nutr Metab 35(4):518-525(2010)Han, S., et al. Hum. Immunol. 71(7):727-730(2010)Rajaraman, P., et al. Cancer Epidemiol. Biomarkers Prev. 19(5):1356-1361(2010)Eeckhoudt, S.L., et al. Thromb. Haemost. 103(4):866-867(2010)Barber, M.J., et al. PLoS ONE 5 (3), E9763 (2010) :
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