K3627
Kallikrein from porcine pancreas
≥40 units/mg protein
Synonym(s):
Kininogenase, Kininogenin
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form
solid
specific activity
≥40 units/mg protein
storage temp.
2-8°C
General description
Kallikrein exists as an inactive prokallikrein in the porcine pancreas. The porcine kallikrein gene region is localized on chromosome 6q12-q21.
Application
Kallikrein from porcine pancreas has been used:
- as a matrix metalloproteinase-9 (MMP-9) zymogen activator
- as a component of cell culture to test its effect on rat subventricular zone (SVZ) cells and oligodendrocyte progenitor cells (OPC) proliferation and survival
- as a model enzyme to track kinetic data and visual detection limits of hydrolysis by hydrolytic enzymes in the two-phases array
Biochem/physiol Actions
Kallikrein active forms are generated by the enzymatic action of trypsin. It is a serine protease that mediates the activation of growth factors and substrates.
Unit Definition
One unit will hydrolyze 1.0 μmole of Nα-benzoyl-L-arginine ethyl ester (BAEE) to Nα-benzoyl-L-arginine and ethanol per min at pH 8.7 at 25°C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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S C Fernando et al.
Genomics, 89(3), 429-438 (2007-01-11)
Kallikreins belong to a family of serine proteases that are widespread throughout living organisms, expressed in diverse tissue-specific patterns, and known to have highly diverse physiological functions. The 15 human and 24 mouse kallikreins have been implicated in pathophysiology of
M G Cotenescu et al.
Journal of biotechnology, 76(1), 33-41 (2000-04-28)
A new assay is described that monitors hydrolysis with the concurrent transfer of a solvatochromic dye across an oil-water barrier. Through the appropriate design, this transfer is accompanied by a 10(6) gain in fluorescence. This response can be used to
Gabriel Rosenblum et al.
Journal of the American Chemical Society, 129(44), 13566-13574 (2007-10-13)
Activation of matrix metalloproteinase zymogen (pro-MMP) is a vital homeostatic process, yet its molecular basis remains unresolved. Using stopped-flow X-ray spectroscopy of the active site zinc ion, we determined the temporal sequence of pro-MMP-9 activation catalyzed by tissue kallikrein protease
Generation of alpha- and beta-kallikreins from porcine pancreatic prokallikrein by the action of trypsin.
M Kamada et al.
Chemical & pharmaceutical bulletin, 36(12), 4891-4899 (1988-12-01)
Prostate-specific antigen kallikrein and non-ST elevation myocardial infarction.
Salvatore Patanè
International journal of cardiology, 149(3), 392-393 (2011-04-01)
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