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anti-Human Cathepsin G Antibodies:
anti-Mouse (Murine) Cathepsin G Antibodies:
anti-Rat (Rattus) Cathepsin G Antibodies:
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Human Monoclonal Cathepsin G Primary Antibody for IHC (p) - ABIN180682
Crocker, Jenkins, Burnett: Immunohistochemical localization of cathepsin G in human tissues. in The American journal of surgical pathology 1986
Show all 2 references for ABIN180682
Human Polyclonal Cathepsin G Primary Antibody for ELISA, WB - ABIN1536111
Salvesen, Farley, Shuman, Przybyla, Reilly, Travis: Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases. in Biochemistry 1987
Data show that lactoferrin (LF (show LTF Antibodies)) increases the catalytic activity of cathepsin G (CatG) at physiological concentration.
CatG is an essential protease for regulating MHC I molecules
Patients with certain polymorphisms in the CTSG gene had lower risk for chronic postsurgical pain compared with wild-types.
These in vivo data provide, for the first time, compelling evidence of the collateral involvement of cathepsin G, NE, and proteinase 3 (show PRTN3 Antibodies) in cigarette smoke-induced tissue damage and emphysema
expression levels of ELANE (show ELANE Antibodies) and CTSG were determined by quantitative real-time PCR
Elastase and cathepsin G are elevated in the plasma of HD patients, originating from primed PMNLs. In these patients, chronic elevation of these enzymes contributes to cleavage of VE-cadherin (show CDH5 Antibodies) and possible disruption of endothelial integrity.
Cathepsin G is an antimicrobial protein with bacteriocidal activity against S. aureus and N. gonorrhoeae.
proteolytic cleavage of PLTP (show PLTP Antibodies) by cathepsin G may enhance the injurious inflammatory responses that occur in COPD (show ARCN1 Antibodies)
Neutrophil cathepsin G is a physiologic modulator of platelet thrombus formation in vivo and has potential as a target for novel anti-thrombotic therapies.
demonstrate that cathepsin G (CG), neutrophil elastase (NE (show ELANE Antibodies)), and to a lesser extent proteinase 3 (PR3 (show PRTN3 Antibodies)), degrade endocan (show ESM1 Antibodies)
Cathepsin G activity may impair efferocytosis, which could lead to an accumulation of lesion-associated apoptotic cells and the accelerated progression of early atherosclerotic lesions to more complex lesions in Apoe (show APOE Antibodies)(-/-) mice.
SerpinB1 (show SERPINB1 Antibodies) is critical for maintaining polymorphonuclear neutrophils survival by antagonizing intracellular cathepsin G activity.
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions.
NADPH oxidase (show NOX1 Antibodies) in antimicrobial host defense against A. fumigatus and B. cepacia, whereas the proteases neutrophil elastase (show ELANE Antibodies), cathepsin G, and lysosomal cysteine protease cathepsin C/ dipeptidyl peptidase I (show CTSC Antibodies) are dispensable
Cathepsin G and neutrophil elastase (show ELANE Antibodies) contribute to lung-protective immunity against mycobacterial infections in mice.
Inhibition of TGF-beta significantly reduces microvessel density in mammary tumor-induced bone lesions, mediated by decreased expression of both vascular endothelial growth factor (VEGF) and monocyte chemotactic protein (MCP)-1.
neutrophil elastase (show ELANE Antibodies) and cathepsin G are inhibited by PAI-1 (show SERPINE1 Antibodies) mutants
cathepsin G activity at the tumor-bone interface plays an important role in mammary tumor-induced osteolysis through RANKL (show TNFSF11 Antibodies)
both Cat-G and PAR(4 (show F2RL3 Antibodies)) play key roles in generating and/or amplifying relapses in ulcerative colitis
Cathepsin G and MMP9 (show MMP9 Antibodies) were identified as proteases involved in enhanced TGF-beta (show TGFB1 Antibodies) signaling at the tumor-bone interface of mammary tumor-induced osteolytic lesions.
The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a 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. Transcript variants utilizing alternative polyadenylation signals exist for this gene.
, vimentin-specific protease