219373
Cathepsin G, Human Neutrophil
Cathepsin G, Human Neutrophil, CAS 107200-92-0, is a purified native cathepsin G. Acts as a potent agonist of human platelet activation leading to their aggregation.
Synonym(s):
Cathepsin G, Human Neutrophil
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77
Recommended Products
biological source
human neutrophils
Quality Level
Assay
≥95% (SDS-PAGE)
form
lyophilized solid (Salt-free)
specific activity
≥2 units/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
technique(s)
inhibition assay: suitable
suitability
suitable for molecular biology
application(s)
life science and biopharma
shipped in
ambient
storage temp.
−20°C
Gene Information
human ... CTSG(1511)
General description
Research area: Cell Signaling
Cathepsin G is stored in its active form in azurophil granules of neutrophils or monocytes. Its mature form contains one potential glycan-binding site and three disulfide bonds.
Cathepsin G is stored in its active form in azurophil granules of neutrophils or monocytes. Its mature form contains one potential glycan-binding site and three disulfide bonds.
Application
Cathepsin G, Human Neutrophil has been used to determine the in vitro bactericidal activities of cathepsin G and for in vitro digestion of plasma/acute wound fluids.
Biochem/physiol Actions
This protease cleaves the triple-helix structure of type I collagen in a restricted manner and degrades nonhelical regions of type I and II collagens, fibronectin, aggrecan, and elastin. Additionally, cathepsin G activates ProMMP-3 and -8. Cathepsin G serves as a chemoattractant for human phagocytes and enhances the random motility of T cells. Additionally, it initiates chemotaxis, activates ERK1/2 and p38 MAPK, and facilitates the translocation of PKCζ to the cell membrane, without inducing a detectable calcium flux. Other biological functions of cathepsin G include: ECM components and plasma proteins degradation, bactericidal actions, cleavage of inflammatory mediators, conversion of angiotensin I to angiotensin II, platelet activation and induction of airway submucosal gland secretion.
Warning
Toxicity: Standard Handling (A)
Unit Definition
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Suc-AAPF-pNA per min at 25°C, pH 7.5.
Preparation Note
Prepared from blood that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Reconstitute in 150 mM NaCl, 50 mM sodium acetate buffer, pH 5.5.
Reconstitute in 150 mM NaCl, 50 mM sodium acetate buffer, pH 5.5.
Reconstitution
Following reconstitution, aliquot and freeze (-70°C) for long term storage or refrigerate (4°C) for short term storage. Stock solutions are stable for up to 1 week at 4°C or for up to 6 months at -70°C.
Reconstitute in 50 mM NaOAc and 150 mM NaCl, pH 5.5.
Other Notes
Glusa, E., and Adam C. 2001. Por. J. Pharmacol.133, 422.
Shamamian, P., et al. 2001. J. Cell Physiol.189, 197.
Groutas, W.C., et al. 1993. Biochem. Biophys. Res. Commun.197, 730.
Stone, P.J., et al. 1993. Biochem. Biophys. Res. Commun.197, 130.
Groutas, W.C., et al. 1992. Arch. Biochem. Biophys.294, 144.
Maison, C.M., et al. 1991. J. Immunol.147, 921.
Travis, J. 1988. Am. J. Med.84, 37.
Shamamian, P., et al. 2001. J. Cell Physiol.189, 197.
Groutas, W.C., et al. 1993. Biochem. Biophys. Res. Commun.197, 730.
Stone, P.J., et al. 1993. Biochem. Biophys. Res. Commun.197, 130.
Groutas, W.C., et al. 1992. Arch. Biochem. Biophys.294, 144.
Maison, C.M., et al. 1991. J. Immunol.147, 921.
Travis, J. 1988. Am. J. Med.84, 37.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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Endogenous and bacterial proteases play important roles in wound healing and infection. Analysis of alterations in the low-molecular-weight peptidome by individual enzymes could therefore provide insight into proteolytic events occurring in wounds and may aid in the discovery of biomarkers.
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Polymorphonuclear neutrophils form a primary line of defense against bacterial infections using complementary oxidative and non-oxidative pathways to destroy phagocytized pathogens. The three serine proteases elastase, proteinase 3 and cathepsin G, are major components of the neutrophil primary granules that
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Although the Streptococcus pneumoniae polysaccharide capsule is an important virulence factor, ~ 15% of carriage isolates are nonencapsulated. Nonencapsulated S. pneumoniae are a cause of mucosal infections. Recent studies have shown that neutrophils kill S. pneumoniae predominately through neutrophil proteases, such as elastase
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