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Human leukocyte cathepsin g

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Human leukocyte cathepsin G is a serine protease enzyme that is primarily found in the azurophilic granules of neutrophils. It plays a role in the degradation of extracellular matrix proteins and the activation of various inflammatory mediators.

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Lab products found in correlation

Human fxa, by Enzyme Research (1 mentions) Heparan sulfate from bovine kidney, by Merck Group (1 mentions) Human thrombin, by Merck Group (1 mentions) Trypsin, by Merck Group (1 mentions) Imac sepharose 6 fast flow, by GE Healthcare (1 mentions) Q5 high fidelity dna polymerase, by New England Biolabs (1 mentions) Human plasmin, by Merck Group (1 mentions) α chymotrypsin from bovine pancreas, by Merck Group (1 mentions) Elastin congo red, by Merck Group (1 mentions) N methoxysuccinyl ala ala pro val p nitroanilide, by Merck Group (1 mentions) N succinyl ala ala pro phe p nitroanilide, by Merck Group (1 mentions) Factor xa, by Prolytix (1 mentions) Plasmin, by Prolytix (1 mentions) Human thrombin, by Prolytix (1 mentions)

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Cathepsin G (9 citations) Human cathepsin G (2 citations) Human leukocytes (2 citations)

3 protocols using human leukocyte cathepsin g

1

Characterizing Cathepsin G Activity

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One U/mL cathepsin G was defined as the concentration of enzyme that releases one nanomole/mL.sec from N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Chromogenix, Antwerp, Belgium), at pH 7.5 and 37 °C. According to this definition, human neutrophil cathepsin G from Calbiochem (95% pure by SDS-PAGE) had a specific activity of 35 U/mg, compared to 60 U/mg for the purified human leukocyte cathepsin G from Sigma.
Nemmar A, & Hoylaerts M.F. (2022). Neutrophil Cathepsin G Enhances Thrombogenicity of Mildly Injured Arteries via ADP-Mediated Platelet Sensitization. International Journal of Molecular Sciences, 23(2), 744.
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2

Characterization of Lamprey AGTR1 Receptor

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Human thrombin (≥2 800 NIH U/ml), human plasmin, human leukocyte cathepsin G, trypsin and α-chymotrypsin from bovine pancreas, affinity-isolated anti-hemagglutinin (HA) antibodies from rabbits and heparan sulfate from bovine kidney were purchased from Sigma-Aldrich. Human FXa (176 IU/mg) was from Enzyme Research Laboratories. Horse anti-mouse IgG and Q5 high-fidelity DNA polymerase (2 000 U/ml) were from New England BioLabs. Horseradish peroxidase-linked anti-rabbit antibodies from donkey and IMAC Sepharose 6 Fast Flow were purchased from GE Healthcare. The FXa substrate S-2222 was from Chromogenix. PCR primers (Table S1) and codon-optimized lamprey AGTR1 DNA fused to EGFP were obtained from Life Technologies GmbH, Darmstadt, Germany. Tetramethylrhodamine-labeled lamprey angiotensin II (TMR-EEDYDERPYMQPF; TMR-angiotensin II for short) was delivered from GenScript Inc., Piscataway, USA.
Wang Y., Köster K., Lummer M, & Ragg H. (2014). Origin of Serpin-Mediated Regulation of Coagulation and Blood Pressure. PLoS ONE, 9(5), e97879.
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3

Enzymatic Assay of Serine Proteases

Cited 1 time
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Human sputum leukocyte elastase was obtained from Elastin Products Company (Owensville, MO). Human thrombin, factor Xa, factor XIa, and plasmin were obtained from Haematologic Technologies (Essex Junction, VT). Human leukocyte cathepsin G, human neutrophil proteinase 3, N-succinyl-Ala-Ala-Val-p-nitroanilide (S1384), N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (S7388), N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide (M4765), elastin-congo red, and bovine pancreatic DNase (DN25) were obtained from Sigma (St. Louis, MO). Low-binding polypropylene 96-well plates for HNE activity assay were from (Greiner Bio One, Monroe, NC. Spectrozyme TH (H-D-cylohexylalanyl-Ala-Arg-p-nitroanilide) and Spectrozyme factor Xa (methoxycarbonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide) were from American Diagnostica (Greenwich, CT). Factor XIa chromogenic substrate (S-2366, L-PyroGlu-Pro-Arg-p-nitroaniline·HCl) was from Diapharma (West Chester, OH). APTT reagent containing ellagic acid (APTT-LS), thromboplastin-D, and 25 mM CaCl2 were obtained from Fisher Diagnostics (Middletown, VA). The library of 60 NSGMs were synthesized with >95% purity using reported schemes30 (link)–32 (link),39 –41 (link) and were characterized by NMR and UPLC-MS.
Morla S., Sankaranarayanan N.V., Afosah D.K., Kumar M., Kummarapurugu A.B., Voynow J.A, & Desai U.R. (2019). On the Process of Discovering Leads that Target the Heparin-Binding Site of Neutrophil Elastase in the Sputum of Cystic Fibrosis Patients. Journal of medicinal chemistry, 62(11), 5501-5511.
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