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AB304943

Human Cathepsin G ELISA Kit

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Human Cathepsin G ELISA Kit is a single-wash 90-min Simplestep used to quantify Human Cathepsin G with a sensitivity of 101.065 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step.

- Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader
- Design your own immunoassay: we also offer the conjugation-ready antibody pair

View Alternative Names

Cathepsin G, CG, CTSG

2 Images
Sandwich ELISA - Human Cathepsin G ELISA Kit (AB304943)
  • sELISA

Supplier Data

Sandwich ELISA - Human Cathepsin G ELISA Kit (AB304943)

Interpolated concentration of native Cathepsin G was measured in duplicate at different sample concentrations. Undiluted samples are as follows : U937 extract 100 µg/mL and HL-60 extract 500 µg/mL. The interpolated dilution factor corrected values are plotted (mean +/- SD, n=2). Sample dilutions are made in 1X Cell Extraction Buffer PTR.

Sandwich ELISA - Human Cathepsin G ELISA Kit (AB304943)
  • sELISA

Supplier Data

Sandwich ELISA - Human Cathepsin G ELISA Kit (AB304943)

Example of human Cathepsin G standard curve. Background-subtracted data values (mean +/- SD) are graphed.

Key facts

Detection method

Colorimetric

Sample types

Cell Lysate

Reacts with

Human

Assay type

Sandwich (quantitative)

Sensitivity

= 101.065 pg/mL

Range

468.75 - 30000 pg/mL

Assay time

1h 30m

Assay Platform

Pre-coated microplate (12 x 8 well strips)

Reactivity data

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Product details

Human Cathepsin G SimpleStep ELISA® kit is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of Cathepsin G protein in human cell extracts and cell lysates. Quantitate Human Cathepsin G with 101.065 pg/ml sensitivity.

SimpleStep ELISA® technology employs capture antibodies conjugated to an affinity tag that is recognized by the monoclonal antibody used to coat our SimpleStep ELISA® plates. This approach to sandwich ELISA allows the formation of the antibody-analyte sandwich complex in a single step, significantly reducing assay time. See the SimpleStep ELISA® protocol summary in the image section for further details. Our SimpleStep ELISA® technology provides several benefits:

-Single-wash protocol reduces assay time to 90 minutes or less
-High sensitivity, specificity and reproducibility from superior antibodies
-Fully validated in biological samples
-96-wells plate breakable into 12 x 8 wells strips

A 384-well SimpleStep ELISA® microplate (ab203359) is available to use as an alternative to the 96-well microplate provided with SimpleStep ELISA® kits.

REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.

Precision

[ { "reproducibilityType": "Intra", "sample": "Extract", "replicates": 8, "mean": null, "standardDeviation": null, "coefficientOfVariability": "9.4" }, { "reproducibilityType": "Inter", "sample": "Extract", "replicates": 3, "mean": null, "standardDeviation": null, "coefficientOfVariability": "11.9" } ]

Recovery

[ { "sample": "Cell Lysate", "range": "95 - 107 %", "average": "= 101" } ]

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
+4°C

Supplementary information

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.
Biological function summary

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.

Pathways

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.

Product protocols

Target data

Serine protease with trypsin- and chymotrypsin-like specificity (PubMed : 29652924, PubMed : 8194606). 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 : 10702240, PubMed : 3390156). 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 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 (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 : 1937776, PubMed : 2116408). 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). Induces platelet aggregation which is strongly potentiated in the presence of ELANE (PubMed : 25211214, PubMed : 9111081).
See full target information Cathepsin G
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