Anti-Cathepsin G Antibody, clone AHN-11, Ascites Free

Format: Purified

Protein G purified

Purified mouse monoclonal IgG2aκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Concentration: Please refer to lot specific datasheet.

Replaces: MAB1054

Evaluated by Immunocytochemistry in HL60 cells.

Immunocytochemistry Analysis: A 1:200 dilution of this antibody detected Cathepsin G in HL60 human promyelocytic leukemia cells.

Research Category
Cell Structure

Research Sub Category
Inflammation & Autoimmune Mechanisms

This Anti-Cathepsin G Antibody, clone AHN-11, Ascites Free is validated for use in Immunocytochemistry, Western Blotting, ELISA, Radioimmunoassay for the detection of Cathepsin G.

Western Blotting Analysis: A representative lot detected cathepsin G in the primary granule fraction from human neutrophils (Stroncek D.F., et al. (2005). J. Transl. Med. 3:36).
Immunocytochemistry Analysis: Clone AHN-11 hybridoma culture supernatant immunostained ethanol-fixed human neutrophils, but not other peripheral blood cells, including platelets, lymphocytes, and eosinophils. Faint immunostaining of some monocytes was occasionally detected (Skubitz, K.M., et al. (1989). J. Leukoc. Biol. 46(2):109-118).
ELISA Analysis: A representative lot captured cathepsin G from human neutrophil granule extract. The captured cathepsin G served to detect the presence of serum cathepsin G autoantibody levels in patients serum samples (Ellerbroek, P.M., et al. (1994). J. Clin. Pathol. 47(3):257-262).
Radioimmunoassay Analysis: Clone AHN-11 hybridoma culture supernatant bound to well surface coated with dried human neutrophils, but not platelets or erythrocytes by solid-phase radioimmunoassay (Skubitz, K.M., et al. (1989). J. Leukoc. Biol. 46(2):109-118).
Radioimmunoassay Analysis: Clone AHN-11 hybridoma culture supernatant bound to well surface coated with content of primary granule, but not secondary granule, plasma membrane, or cytoplasm fraction from neutrophils by solid-phase radioimmunoassay (Skubitz, K.M., et al. (1989). J. Leukoc. Biol. 46(2):109-118).
Radioimmunoassay Analysis: Clone AHN-11 hybridoma culture supernatant reacted with purified human cathepsin G, but not elastase, EPO, esterase N, proteinase 3, plamin, kallidrein, lactoferrin, MBP, or thrombin by solid-phase radioimmunoassay (Skubitz, K.M., et al. (1989). J. Leukoc. Biol. 46(2):109-118).

Clone AHN-11 reacted specifically with neutrophil cathepsin G, but not the homologous neutrophil neutral proteases, elastase, proteinase 3, or esterase N (Skubitz, K.M., et al. (1989). J. Leukoc. Biol. 46(2):109-118).

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

28.84 kDa (prepro-form; a.a. 1-255), 26.94 kDa (pro-form; a.a. 19-255), 26.76 kDa (active form; a.a. 21-255) calculated.

Cathepsin G (EC 3.4.21.20; UniProt P08311; also known as CatG, CG) is encoded by the CTSG gene (Gene ID 1511) in human. Cathepsin G is a peptidase S1 protein family protease found in azurophil granules of neutrophilic polymorphonuclear leukocytes. Cathepsin G displays a substrate specificity similar to that of chymotrypsin C, but it is most closely related to other immune serine proteases, such as neutrophil elastase and the granzymes. Cathepsin G is involved in connective tissue remodeling at sites of inflammation. Cathepsin G is also a component of neutrophil extracellular traps (NETs) composed of ejected lattice of chromatin enmeshed with granular and nuclear proteins, including histones, calprotectin and cathepsin G, that are capable of capturing and killing microbial invaders. Antibodies raised against cathepsin G or histones have been shown to limit the bactericidal capacity of NETs towards pathogens. Cathepsin G is prouduced with a signal peptide (a.a. 1-18) and a propeptide sequence (a.a. 19-20) that are removed posttranslationally to yield the mature (a.a. 21-255) enzyme.

Human neutrophils.

Stable for 1 year at 2-8°C from date of receipt.