K3627
Kallikrein from porcine pancreas
≥40 units/mg protein
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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
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
动植物源性产品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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)
Duncan J Campbell et al.
Clinical and experimental pharmacology & physiology, 38(9), 623-631 (2011-07-09)
1. Aliskiren is a renin inhibitor with an IC(50) of 0.6 nmol/L for human renin, 4.5 nmol/L for mouse renin and 80 nmol/L for rat renin. 2. In the present study, we compared the effects of aliskiren (10 mg/kg per day)
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