Cathepsin G Antibody
(Synonyms: Cathepsin G, CG, CTSG)Cathepsin G Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to Cathepsin G.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
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Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:50-200 |
Product Details
Cathepsin G Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to Cathepsin G.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
Synthetic peptide corresponding to the N-term region of human Cathepsin G.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Cathepsin G is a Serine protease with trypsin- and chymotrypsin-like specificity. Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity. Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu. 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. Required for recruitment and activation of platelets which is mediated by the F2RL3/PAR4 platelet receptor. Binds reversibly to and stimulates B cells and CD4(+) and CD8(+) T cells. Also binds reversibly to natural killer (NK) cells and enhances NK cell cytotoxicity through its protease activity. Cleaves complement C3. Cleaves vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts as either an agonist or an inhibitor, depending on the F2R cleavage site. 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. Cleaves the synovial mucin-type protein PRG4/lubricin. Cleaves and activates IL36G which promotes expression of chemokines CXCL1 and CXLC8 in keratinocytes. Cleaves IL33 into mature forms which have greater activity than the unprocessed form. Cleaves coagulation factor F8 to produce a partially activated form. Also cleaves and activates coagulation factor F10. Cleaves leukocyte cell surface protein SPN/CD43 to release its extracellular domain and trigger its intramembrane proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus. Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal three amino acids which exhibits reduced chemotactic and antiviral activities. During apoptosis, cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which localizes to the cytosol. 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. Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce peptides which act on neutrophil N-formyl peptide receptors to enhance the release of CXCL2. Acts as a ligand for the N-formyl peptide receptor FPR1, enhancing phagocyte chemotaxis. Has antibacterial activity against the Gram-negative bacteria N.gonorrhoeae and P.aeruginosa. Likely to act against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2. Exhibits potent antimicrobial activity against the Gram-positive bacterium L.monocytogenes. 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. Has antibacterial activity against M.tuberculosis. 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. Induces platelet aggregation which is strongly potentiated in the presence of ELANE[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29].
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Subcellular Localization
Cell membrane; Cytoplasmic granule; Secreted; Cytoplasm, cytosol; Lysosome; Nucleus
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Expression
Tissue_Specificity: Expressed in neutrophils (at protein level). Expressed in B cells.
Induction: Induced by the Td92 surface protein of the periodontal pathogen T.denticola. Down-regulated in monocytes following M.tuberculosis infection and exposure to bacterial lipopolysaccharide which coincides with increased M.tuberculosis replication and intracellular survival. -
Isoforms & Post-Translational Modification
Cathepsin G has an amino acid length of 255, molecular weight is 28837 Da.
Two C-terminal truncation variants have been identified, one which ends at Arg-243 and one which ends at Ser-244. -
Subunit
(Microbial infection) Interacts with CASP4; the interaction is promoted by the Td92 surface protein of the periodontal pathogen T.denticola and leads to CASP4 activation
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SwissProt ID
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Synonyms
Cathepsin G, CG, CTSG
Documentation
References
[1]. Thorpe M, et al. Extended cleavage specificity of human neutrophil cathepsin G: A low activity protease with dual chymase and tryptase-type specificities. PLoS One. 2018;13(4):e0195077. [Content Brief]
[2]. Avril LE, et al. Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. FEBS Lett. 1994 May 23;345(1):81-6. [Content Brief]
[3]. Bangalore N, et al. Identification of the primary antimicrobial domains in human neutrophil cathepsin G. J Biol Chem. 1990 Aug 15;265(23):13584-8. [Content Brief]
[4]. Alford CE, et al. Listericidal activity of human neutrophil cathepsin G. J Gen Microbiol. 1990 Jun;136(6):997-100. [Content Brief]
[5]. Sambrano GR, et al. Cathepsin G activates protease-activated receptor-4 in human platelets. J Biol Chem. 2000 Mar 10;275(10):6819-23. [Content Brief]
[6]. Selak MA, et al. Cathepsin G is a strong platelet agonist released by neutrophils. Biochem J. 1988 Apr 1;251(1):293-9. [Content Brief]
[7]. Hase-Yamazaki T, et al. Stimulation of human lymphocytes by cathepsin G. Cell Immunol. 1995 Jan;160(1):24-32. [Content Brief]
[8]. Yamazaki T, et al. Cathepsin G binds to human lymphocytes. J Leukoc Biol. 1997 Jan;61(1):73-9. [Content Brief]
[9]. Yamazaki T, et al. Cathepsin G enhances human natural killer cytotoxicity. Immunology. 1998 Jan;93(1):115-21. [Content Brief]
[10]. Maison CM, et al. Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J Immunol. 1991 Aug 1;147(3):921-6. [Content Brief]
[11]. Molino M, et al. Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G. J Biol Chem. 1995 May 12;270(19):11168-75. [Content Brief]
[12]. Huang S, et al. Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of Lubricin, a Synovial Mucin. Sci Rep. 2020 Mar 6;10(1):4215. [Content Brief]
[13]. Guo J, et al. Cathepsin G cleaves and activates IL-36γ and promotes the inflammation of psoriasis. Drug Des Devel Ther. 2019;13:581-588. [Content Brief]
[14]. Lefrançais E, et al. IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G. Proc Natl Acad Sci U S A. 2012 Jan 31;109(5):1673-8. [Content Brief]
[15]. Gale AJ, et al. Cathepsin G, a leukocyte protease, activates coagulation factor VIII. Thromb Haemost. 2008 Jan;99(1):44-51. [Content Brief]
[16]. Plescia J, et al. Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation. Biochem J. 1996 Nov 1;319 ( Pt 3)(Pt 3):873-9. [Content Brief]
[17]. Mambole A, et al. The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase. J Biol Chem. 2008 Aug 29;283(35):23627-35. [Content Brief]
[18]. Lim JK, et al. N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant. J Leukoc Biol. 2006 Dec;80(6):1395-404. [Content Brief]
[19]. Biggs JR, et al. The human brm protein is cleaved during apoptosis: the role of cathepsin G. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3814-9. [Content Brief]
[20]. Burster T, et al. Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. J Immunol. 2004 May 1;172(9):5495-503. [Content Brief]
[21]. Woloszynek JC, et al. Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions. J Biol Chem. 2012 Oct 5;287(41):34101-9. [Content Brief]
[22]. Sun R, et al. Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor. J Immunol. 2004 Jul 1;173(1):428-36. [Content Brief]
[23]. Wasiluk KR, et al. Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. Infect Immun. 1991 Nov;59(11):4193-200. [Content Brief]
[24]. Shafer WM, et al. Molecular mechanism for the antigonococcal action of lysosomal cathepsin G. Mol Microbiol. 1990 Aug;4(8):1269-77. [Content Brief]
[25]. Kavanaugh JS, et al. Cathepsin G Degrades Staphylococcus aureus Biofilms. J Infect Dis. 2021 Jun 4;223(11):1865-1869. [Content Brief]
[26]. Rivera-Marrero CA, et al. The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli. Infect Immun. 2004 Oct;72(10):5712-21. [Content Brief]
[27]. Jun HK, et al. Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts. Cell Death Differ. 2018 Feb;25(2):380-391. [Content Brief]
[28]. Waisberg M, et al. Plasmodium falciparum infection induces expression of a mosquito salivary protein (Agaphelin) that targets neutrophil function and inhibits thrombosis without impairing hemostasis. PLoS Pathog. 2014 Sep;10(9):e1004338. [Content Brief]
[29]. Si-Tahar M, et al. Human neutrophil elastase proteolytically activates the platelet integrin alphaIIbbeta3 through cleavage of the carboxyl terminus of the alphaIIb subunit heavy chain. Involvement in the potentiation of platelet aggregation. J Biol Chem. 1997 Apr 25;272(17):11636-47. [Content Brief]
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