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About This Item
CAS Number:
UNSPSC Code:
12352200
NACRES:
NA.32
MDL number:
Product Name
Cathepsin G from human leukocytes, lyophilized powder, ≥60 units/mg protein (Bradford)
biological source
human leucocytes
form
lyophilized powder
specific activity
≥60 units/mg protein (Bradford)
mol wt
23-30 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CTSG(1511)
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Physical form
Lyophilized from 0.5 M pyridinium acetate, pH 5.3.
Application
Cathepsin G from human leukocytes has been used to determine protease sensitivity. It has also been used for the stimulation and staining of dendritic cells and macrophage.
Biochem/physiol Actions
Cathepsin G from human leukocytes degrades various proteins, such as elastin, collagen, fibrinogen and immunoglobin. It may be implicated in muscle catabolism. Cathepsin G is involved in the activation or inactivation of protein hormones and the inactivation of plasma proteinase inhibitors. It alters the cytoskeleton, enhances the permeability of vascular endothelial cells and the chemotaxis of inflammatory cells. Cathepsin G is associated with autoimmunity and cancer. It exhibits chymotrypsin and trypsin like activity. Cathepsin G modulates neutrophil effector functions.
Cathepsin G has pro-apoptotic activity and can activate caspases in vitro.
General description
Cathepsin G from human leukocytes is a neutral proteinase secreted by neutrophil granulocytes. It belongs to the family of serine proteases. Cathepsin G is a glycoprotein, which contains 1% carbohydrate. The gene is located on human chromosome 14q12.
Other Notes
One unit will release one nanomole of p-nitroaniline per second from N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide at pH 7.5 at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Structure, function, and control of neutrophil proteinases
Travis J
The American Journal of Medicine, 84(6), 37-42 (1988)
Cathepsin G: roles in antigen presentation and beyond
Burster T, et al.
Molecular Immunology, 47(4), 658-665 (2010)
Delivery and therapeutic potential of human granzyme B
Kurschus FC and Jenne DE
Immunological Reviews, 235(1), 159-171 (2010)
A type VII collagen subdomain mutant is thermolabile and shows enhanced proteolytic degradability?Implications for the pathogenesis of recessive dystrophic epidermolysis bullosa?
Windler C, et al.
Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1863(1), 52-59 (2017)
P I Bird
Immunology and cell biology, 77(1), 47-57 (1999-04-02)
Caspase activation and apoptosis can be initiated by the introduction of serine proteinases into the cytoplasm of a cell. Cytotoxic lymphocytes have evolved at least one serine proteinase with specific pro-apoptotic activity (granzyme B), as well as the mechanisms to
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