K3627
Kallikrein from porcine pancreas
≥40 units/mg protein
Synonyme(s) :
Kininogenase, Kininogenin
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About This Item
Produits recommandés
Forme
solid
Activité spécifique
≥40 units/mg protein
Température de stockage
2-8°C
Description générale
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
Actions biochimiques/physiologiques
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.
Définition de l'unité
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.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (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
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)
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
Hui-Zhen Yu et al.
Molecular and cellular biochemistry, 360(1-2), 363-371 (2011-10-01)
Tissue kallikrein 1 cleaves kininogen substrate to produce vasoactive kinin peptides that have been implicated in inhibiting neointimal hyperplasia in rat carotid arteries after balloon injury. However, its effects on the proliferation, cell cycle and its mechanisms, for example, cyclin-dependent
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