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Cathepsin G (human neutrophils), (purified)

BML-SE283-0100 100 µg 399.00 USD
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Replaces Prod. #: ALX-200-310

Product Details

Source:Isolated from human neutrophils. Active enzyme. Negative for HbsAg, anti-HBc, anti-HCV, and anti-HIV-1 and -2.
UniProt ID:P08311
Purity:≥95% by SDS-PAGE
Specific Activity:2 to 4 units per mg protein. One unit of activity is defined as the amount of enzyme that hydrolyzes one micromole of Suc-Ala-Ala-Pro-Phe-pNA (1mM) per minute at 25°C in 160mM TRIS-HCl, pH 7.4, containing 1.6M sodium chloride.
Application Notes:Useful for inhibitor screening, kinetic studies, and cleavage of substrates in vitro or in tissue culture.
Reconstitution:Reconstitute with 50 mM sodium acetate, pH5.5, containing 150 mM NaCl.
Shipping:Dry Ice
Long Term Storage:-80°C
Scientific Background:Cathepsin G, a serine protease found in polymorphonuclear neutrophils (PMNs), functions in inflammation.
Regulatory Status:RUO - Research Use Only

Product Literature References

The Stressed Gut: Region-specific Immune and Neuroplasticity Changes in Response to Chronic Psychosocial Stress: B. Lobo, et al.; J. Neurogastroenterol. Motil. 29, 72 (2023), Abstract;
Protective role of casuarinin from Melastoma malabathricum against a mouse model of 5-fluorouracil–induced intestinal mucositis: Impact on inflammation and gut microbiota dysbiosis: K.J. Chen, et al.; Phytomedicine 101, 154092 (2022), Abstract;
Lignosulfonic Acid Sodium Is a Noncompetitive Inhibitor of Human Factor Xia: S. Kar, et al.; Pharmaceuticals 14, 886 (2021), Abstract;
Cathepsin G cleaves and activates IL-36γ and promotes the inflammation of psoriasis: J. Guo, et al.; Drug Des. Devel. Ther. 13, 581 (2019), Application(s): stimulate HaCaT response w/ different dosing of Cathepsin G, Abstract; Full Text
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L: D. Dana, et al.; Bioorg. Chem. 85, 505 (2019), Application(s): Activity assay, Abstract;
Discovery and validation of 2-styryl substituted benzoxazin-4-ones as a novel scaffold for rhomboid protease inhibitors: P. Goel, et al.; Bioorg. Med. Chem. Lett. 28, 1417 (2018), Abstract;
The putative role of Rhipicephalus microplus salivary serpins in the tick-host relationship: L. Tirloni, et al.; Insect Biochem. Mol. Biol. 71, 12 (2016), Application(s): Protease inhibition assay, Abstract;
Development of a highly potent, selective, and cell-active Inhibitor of cysteine cathepsin L-A hybrid design approach: D. Dana, et al.; Chem. Commun. (Camb.) 50, 10875 (2014), Abstract;
Development of cell-active non-peptidyl inhibitors of cysteine cathepsins: D. Dana, et al.; Bioorg. Med. Chem. 21, 2975 (2013), Abstract;

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