Cathepsin G - 0.2mg

Cathepsin G - 0.2mg

$252.84
$252.84
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Cathepsin GCTSG

Uniprot ID:  P08311
mRNA RefSeq:  NM_001911
Protein RefSeq:  NP_001902
Size: 0.2mg
Source: Human Neutrophils
Catalogue Number: ATC01-02

 

Product Information

Cathepsin G is a member of the hematopoietic serine proteinase super family along with elastase and proteinase 3. Cathepsin G, a 225 amino acid residue protein with an 18 residue signal peptide and a 2 residue activation peptide at the N-terminus, is a ubiquitous enzyme secreted by neutrophils. These serine proteases are mainly stored in the azurophilic granules and are activated by dipeptidyl peptidase 1 during neutrophil activation. Independent of its proteinase activity, cathepsin G is a significant broad spectrum anti-microbial agent.

There is published data that ANCA associated antibodies against cathepsin G are found in ulcerative colitis and crohn’s disease. It is thought to have a stronger association with ulcerative colitis activity than either primary sclerosing cholangitis or crohn’s disease. Cathepsin G is also present in some vasculitic diseases but is not as specific or as prevalent a marker as MPO and PR3.

 

PDF-logo-dl Cathepsin G datasheet

Clinical Indications

Primary Sclerosing Cholangitis
Crohn's disease
Ulcerative Colitis
Cathepsin G is implicated in cardiovascular and cerebrovascular diseases

MSDS

PDF-logo-dl  Material Safety Data Sheet

References

Watorek W. et al. (1988) Neutrophil elastase and cathepsin G: structure, function, and biological control. Adv. Exp. Med. Biol. 240:23-31

Hof P. et al. (1996) The 8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities. EMBO J. 15:5481-91

Polanowska J. et al. (1998) Specificity of human cathepsin G. Biochim. Biophys. Acta 1386:189-98

Korkmaz B. et al. (2008) Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions.Biochimie 90:227-42

Sepper R. et al. (1995) Presence, activities, and molecular forms of cathepsin G, elastase, alpha 1-antitrypsin, and alpha 1-antichymotrypsin in bronchiectasis. J. Clin. Immunol. 15:27-34

Tervahartiala T. et al. (1996) Cathepsin G in gingival tissue and crevicular fluid in adult periodontosis. J. Clin. Periodontol. 23:68-75

Tamiya H. et al. (2006) Defensins- and cathepsin G-ANCA in systemic lupus erythematosus. Rheumatol. Int. 27:147-52

Khanna D. et al. (2003) Bactericidal/permeability-increasing protein and cathepsin G are the major antigenic targets of antineutrophil cytoplasmic autoantibodies in systemic sclerosis. J. Rheumatol. 30:1248-52

Halbwachs-Mecarelli L. et al. (1992) Antineutrophil cytoplasmic antibodies (ANCA) directed against cathepsin G in ulcerative colitis, Crohn's disease and primary sclerosing cholangitis. Clin. Exp. Immunol. 90:79-84

Kuwana T. et al. (2000) Anti-cathepsin G antibodies in the sera of patients with ulcerative colitis. J. Gastroenterol. 35:682-9

Yahya T.M. et al. (1997) Anti-neutrophil cytoplasmic antibody (ANCA) in malaria is directed against cathepsin G. Clin. Exp. Immunol. 110:41-4