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Sigma-Aldrich

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.

Synonyme(s) :

Cathepsin G, Human Neutrophil

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

Source biologique

human neutrophils

Niveau de qualité

Pureté

≥95% (SDS-PAGE)

Forme

lyophilized solid (Salt-free)

Activité spécifique

≥2 units/mg protein

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Technique(s)

inhibition assay: suitable

Adéquation

suitable for molecular biology

Application(s)

life science and biopharma

Conditions d'expédition

ambient

Température de stockage

−20°C

Informations sur le gène

human ... CTSG(1511)

Description générale

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.

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.

Actions biochimiques/physiologiques

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.

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

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.

Notes préparatoires

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.

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.

Autres remarques

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.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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


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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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