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.
Sinónimos:
Cathepsin G, Human Neutrophil
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About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.77
Productos recomendados
origen biológico
human neutrophils
Nivel de calidad
descripción
Merck USA index - 14, 1905
Ensayo
≥95% (SDS-PAGE)
Formulario
lyophilized solid (Salt-free)
actividad específica
≥2 units/mg protein
fabricante / nombre comercial
Calbiochem®
condiciones de almacenamiento
OK to freeze
técnicas
inhibition assay: suitable
idoneidad
suitable for molecular biology
aplicaciones
life science and biopharma
Condiciones de envío
ambient
temp. de almacenamiento
−20°C
Información sobre el gen
human ... CTSG(1511)
Descripción general
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.
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Advertencia
Toxicity: Standard Handling (A)
Definición de unidad
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.
Nota de preparación
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.
Reconstitución
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.
Otras notas
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.
Información legal
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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