Cathepsin G Inhibitor Screening Assay Kit (Colorimetric) (ab204693) uses the ability of active Cathepsin G to cleave a synthetic pNA (4-Nitroaniline)-based peptide substrate to release pNA, which can be easily quantified using a colorimetric microplate reader.
Colorimetric
Inhibitor compounds
Enzyme activity
Select an associated product type
Serine protease with trypsin- and chymotrypsin-like specificity (PubMed:8194606, PubMed:29652924). Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity (PubMed:2116408, PubMed:2117044). Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu (PubMed:29652924). Shows a preference for negatively charged amino acids in the P2' position and for aliphatic amino acids both upstream and downstream of the cleavage site (PubMed:29652924). Required for recruitment and activation of platelets which is mediated by the F2RL3/PAR4 platelet receptor (PubMed:3390156, PubMed:10702240). Binds reversibly to and stimulates B cells and CD4(+) and CD8(+) T cells (PubMed:7842483, PubMed:9000539). Also binds reversibly to natural killer (NK) cells and enhances NK cell cytotoxicity through its protease activity (PubMed:9000539, PubMed:9536127). Cleaves complement C3 (PubMed:1861080). Cleaves vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts as either an agonist or an inhibitor, depending on the F2R cleavage site (PubMed:10702240, PubMed:7744748). Cleavage of F2R at '41-Arg-|-Ser-42' results in receptor activation while cleavage at '55-Phe-|-Trp-56' results in inhibition of receptor activation (PubMed:7744748). Cleaves the synovial mucin-type protein PRG4/lubricin (PubMed:32144329). Cleaves and activates IL36G which promotes expression of chemokines CXCL1 and CXLC8 in keratinocytes (PubMed:30804664). Cleaves IL33 into mature forms which have greater activity than the unprocessed form (PubMed:22307629). Cleaves coagulation factor F8 to produce a partially activated form (PubMed:18217133). Also cleaves and activates coagulation factor F10 (PubMed:8920993). Cleaves leukocyte cell surface protein SPN/CD43 to releases its extracellular domain and trigger its intramembrane proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus (PubMed:18586676). Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal three amino acids which exhibits reduced chemotactic and antiviral activities (PubMed:16963625). During apoptosis, cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which localizes to the cytosol (PubMed:11259672). Cleaves myelin basic protein MBP in B cell lysosomes at '224-Phe-|-Lys-225' and '248-Phe-|-Ser-249', degrading the major immunogenic MBP epitope and preventing the activation of MBP-specific autoreactive T cells (PubMed:15100291). Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce peptides which act on neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Acts as a ligand for the N-formyl peptide receptor FPR1, enhancing phagocyte chemotaxis (PubMed:15210802). Has antibacterial activity against the Gram-negative bacteria N.gonorrhoeae and P.aeruginosa (PubMed:2116408, PubMed:1937776). Likely to act against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2 (PubMed:2126324). Exhibits potent antimicrobial activity against the Gram-positive bacterium L.monocytogenes (PubMed:2117044). Has antibacterial activity against the Gram-positive bacterium S.aureus and degrades S.aureus biofilms, allowing polymorphonuclear leukocytes to penetrate the biofilm and phagocytose bacteria (PubMed:2117044, PubMed:32995850). Has antibacterial activity against M.tuberculosis (PubMed:15385470). Mediates CASP4 activation induced by the Td92 surface protein of the periodontal pathogen T.denticola, causing production and secretion of IL1A and leading to pyroptosis of gingival fibroblasts (PubMed:29077095).
Cathepsin G, CG, CTSG
Cathepsin G Inhibitor Screening Assay Kit (Colorimetric) (ab204693) uses the ability of active Cathepsin G to cleave a synthetic pNA (4-Nitroaniline)-based peptide substrate to release pNA, which can be easily quantified using a colorimetric microplate reader.
Cathepsin G, CG, CTSG
Colorimetric
Inhibitor compounds
Enzyme activity
Microplate reader
Blue Ice
-20°C
-20°C
-20°C
Cathepsin G Inhibitor Screening Assay Kit (Colorimetric) (ab204693) uses the ability of active Cathepsin G to cleave a synthetic pNA (4-Nitroaniline)-based peptide substrate to release pNA, which can be easily quantified using a colorimetric microplate reader. In the presence of a Cathepsin G inhibitor, the cleavage of this substrate is reduced/abolished resulting in decrease or total loss of the pNA absorbance. This simple and high-throughput adaptable assay kit can be used to screen/study/characterize potential inhibitors of Cathepsin G.
This product is manufactured by BioVision, an Abcam company and was previously called K162 Cathepsin G Inhibitor Screening Kit (Colorimetric). K162-100 is the same size as the 100 test size of ab204693.
Cathepsin G (CTSG, EC 3.4.21.20) is a Serine protease found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation.
This supplementary information is collated from multiple sources and compiled automatically.
Cathepsin G also known as CTSG is a serine protease with a molecular mass of approximately 29 kDa. It is primarily located in azurophilic granules of neutrophils a type of white blood cell. Cathepsin G functions mechanically as an enzyme cleaving peptide bonds in proteins and shaping the protein components involved in various immune responses. Its enzymatic activity is important for host defense processes including bacterial degradation and immune cell signaling. Researchers easily measure and study 'G activity' using specific functional assays.
Cathepsin G plays a significant role in the immune system by contributing to inflammatory responses and regulating cellular processes through its proteolytic activity. It participates in activating other proteins such as anti-bacterial serine enzymes and breaking down extracellular matrix components during immune response facilitation. While not part of a larger complex cathepsin G works alongside other proteases showing combinatory effects in innate immunity.
Cathepsin G is involved in the immune and inflammatory pathways. It plays a part in the regulation of inflammatory responses and contributes to the activation of cytokines during infection and tissue injury. Cathepsin G connects through shared activity with other proteases like neutrophil elastase influencing processes in tissue remodeling and cytokine release. It sustains immune system homeostasis maintaining a balance between inflammation and tissue repair in these pathways.
Cathepsin G is linked to chronic inflammatory conditions and autoimmune disorders. For example rheumatoid arthritis showcases the enzyme's connection where cathepsin G contributes to tissue damage and joint inflammation. Cathepsin G's increased activity associates with neutrophil elastase aggravating symptoms of chronic obstructive pulmonary disease (COPD) as it contributes to lung tissue degradation. Understanding cathepsin G's role in these diseases aids research in therapeutic target development focusing on 'E-64d' inhibitors. These inhibitors reduce inflammatory damage by curbing excessive protease activity.
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Inhibition of Cathepsin G activity by CTSG Inhibitor.
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