Plasma prekallikrein is a glycoprotein that participates
in the surface-dependent activation of blood coagulation,
fibrinolysis, kinin generation and inflammation. It is synthesized
in the liver and secreted into the blood as a single polypeptide
chain. Plasma prekallikrein is converted to plasma kallikrein by
factor XIIa by the cleavage of an internal Arg-Ile bond. Plasma
kallikrein therefore is composed of a heavy chain and a light chain
held together by a disulphide bond. The heavy chain originates
from the amino-terminal end of the zymogen and contains 4 tandem
repeats of 90 or 91 amino acids. Each repeat harbors a novel
structure called the apple domain. The heavy chain is required for
the surface-dependent pro-coagulant activity of plasma kallikrein.
The light chain contains the active site or catalytic domain of the
enzyme and is homologous to the trypsin family of serine proteases.
Plasma prekallikrein deficiency causes a prolonged activated
partial thromboplastin time in patients.1) MacKenzie, J.A., et al. Appl Physiol Nutr Metab 35(4):518-525(2010)
Immunogen
This KLKB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 508-537 amino acids from the C-terminal region of human KLKB1.
Western blot analysis in K562 cell line lysates (35ug/lane).
Application Notes
For WB starting dilution is: 1:1000
Additional Information
Form
Liquid
Storage Instructions
Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.