C4428
Cathepsin G from human leukocytes
lyophilized powder, ≥60 units/mg protein (Bradford)
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.32
Recommended Products
biological source
human leucocytes
Quality Level
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
Gene Information
human ... CTSG(1511)
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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.
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.
Unit Definition
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.
Physical form
Lyophilized from 0.5 M pyridinium acetate, pH 5.3.
inhibitor
substrate
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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)
Delivery and therapeutic potential of human granzyme B
Kurschus FC and Jenne DE
Immunological Reviews, 235(1), 159-171 (2010)
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)
Cell surface cathepsin G activity differs between human natural killer cell subsets
Penczek A, et al.
Immunology Letters, 179, 80-84 (2016)
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