Review



cathepsin g cg  (Valiant Co Ltd)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    Valiant Co Ltd cathepsin g cg
    Cathepsin G Cg, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/0219134480/Cathepsin+G/pm22465040-49-27-34
    Average 90 stars, based on 16 article reviews
    cathepsin g cg - by Bioz Stars, 2026-09
    90/100 stars

    Images

    Related Articles

    Membrane:

    Article Title: Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils
    Article Snippet: Percent survival is depicted as the percent survival of Gc during antimicrobial treatment divided by the percent survival of Gc during vehicle control treatment to normalize to vehicle-treated bacteria. . Lysozyme Gc was incubated with indicated concentrations of human lysozyme (Sigma) reconstituted in water for 3 hr or otherwise indicated. .. Cathepsin G (MP Biomedicals) was prepared for use by overnight dialysis at 4°C in distilled water using SpectraPor dialysis membrane MW cutoff 3500 (Spectrum labs). .. For lysozyme treatment with EDTA, GC was incubated with the indicated concentrations of lysozyme in the presence of 1mM EDTA for 30 min. . Mutanolysin Gc was incubated with indicated concentrations of mutanolysin (Sigma) reconstituted in 100mM potassium phosphate buffer, pH 6.2 for 3 hr. . Neutrophil Elastase (NE) Gc was incubated with indicated concentrations of NE (Sigma) reconstituted in 0.5× GCBL for 3 hr.

    Article Title: Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils
    Article Snippet: For treatment with a protease inhibitor cocktail, NE and vehicle control was incubated with 1× strength protease inhibitor cocktail set V (Millipore) for 30 min at 37°C prior to incubation with Gc. .. Azurocidin Gc was incubated with indicated concentrations of Azurocidin (Sigma) reconstituted in 0.5× GCBL for 45 min. Human Neutrophil Peptide-1 (HNP-1) Gc was incubated with indicated concentrations of the α-defensin HNP-1 (Sigma) reconstituted in 0.5× GCBL for 45 min. LL-37 Gc was incubated with indicated concentrations of LL-37 (from William Shafer, Emory University) diluted in water for 45 min. Bactericidal Permeability-Increasing Protein (BPI) Gc was incubated with indicated concentrations of BPI (Novatein Biosciences) diluted in 0.01% acetic acid for 45 min. Cathepsin G Cathepsin G (MP Biomedicals) was prepared for use by overnight dialysis at 4°C in distilled water using SpectraPor dialysis membrane MW cutoff 3500 (Spectrum labs). ..

    Incubation:

    Article Title: Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils
    Article Snippet: For treatment with a protease inhibitor cocktail, NE and vehicle control was incubated with 1× strength protease inhibitor cocktail set V (Millipore) for 30 min at 37°C prior to incubation with Gc. .. Azurocidin Gc was incubated with indicated concentrations of Azurocidin (Sigma) reconstituted in 0.5× GCBL for 45 min. Human Neutrophil Peptide-1 (HNP-1) Gc was incubated with indicated concentrations of the α-defensin HNP-1 (Sigma) reconstituted in 0.5× GCBL for 45 min. LL-37 Gc was incubated with indicated concentrations of LL-37 (from William Shafer, Emory University) diluted in water for 45 min. Bactericidal Permeability-Increasing Protein (BPI) Gc was incubated with indicated concentrations of BPI (Novatein Biosciences) diluted in 0.01% acetic acid for 45 min. Cathepsin G Cathepsin G (MP Biomedicals) was prepared for use by overnight dialysis at 4°C in distilled water using SpectraPor dialysis membrane MW cutoff 3500 (Spectrum labs). ..

    Permeability:

    Article Title: Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils
    Article Snippet: For treatment with a protease inhibitor cocktail, NE and vehicle control was incubated with 1× strength protease inhibitor cocktail set V (Millipore) for 30 min at 37°C prior to incubation with Gc. .. Azurocidin Gc was incubated with indicated concentrations of Azurocidin (Sigma) reconstituted in 0.5× GCBL for 45 min. Human Neutrophil Peptide-1 (HNP-1) Gc was incubated with indicated concentrations of the α-defensin HNP-1 (Sigma) reconstituted in 0.5× GCBL for 45 min. LL-37 Gc was incubated with indicated concentrations of LL-37 (from William Shafer, Emory University) diluted in water for 45 min. Bactericidal Permeability-Increasing Protein (BPI) Gc was incubated with indicated concentrations of BPI (Novatein Biosciences) diluted in 0.01% acetic acid for 45 min. Cathepsin G Cathepsin G (MP Biomedicals) was prepared for use by overnight dialysis at 4°C in distilled water using SpectraPor dialysis membrane MW cutoff 3500 (Spectrum labs). ..



    Similar Products

    cathepsin g cathepsin g  (Valiant Co Ltd)
    90
    Valiant Co Ltd cathepsin g cathepsin g
    Cathepsin G Cathepsin G, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/0219134480/Cathepsin+G/pmc05303151-467-81-85
    Average 90 stars, based on 1 article reviews
    cathepsin g cathepsin g - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier
    cathepsin g  (Valiant Co Ltd)
    90
    Valiant Co Ltd cathepsin g
    Cathepsin G, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/0219134480/Cathepsin+G/pmc05303151-610-0-2
    Average 90 stars, based on 1 article reviews
    cathepsin g - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier
    neutrophil cathepsin g  (Valiant Co Ltd)
    90
    Valiant Co Ltd neutrophil cathepsin g
    Neutrophil Cathepsin G, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/0219134480/Cathepsin+G/pm27562418-51-7-10
    Average 90 stars, based on 1 article reviews
    neutrophil cathepsin g - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier
    human cathepsin g  (Valiant Co Ltd)
    90
    Valiant Co Ltd human cathepsin g
    Aligned portions of the catalytic domains (amino acids 185–220 using standard chymotrypsinogen numbering) bracket specificity-determining “triad” residues 189, 216, and 226 (shaded). Ser195 involved in hydrolysis is marked with an asterisk. Hyphens indicate identity with human sequence. Human <t>cathepsin</t> <t>G</t> differs from consensus at two of three (Ala189 and Glu226) specificity triad residues (58). Mouse cathepsin G and most other mammalian proteases match consensus sequence at these residues (59).
    Human Cathepsin G, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/0219134480/Cathepsin+G/pmc03954857-82-0-3
    Average 90 stars, based on 1 article reviews
    human cathepsin g - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Aligned portions of the catalytic domains (amino acids 185–220 using standard chymotrypsinogen numbering) bracket specificity-determining “triad” residues 189, 216, and 226 (shaded). Ser195 involved in hydrolysis is marked with an asterisk. Hyphens indicate identity with human sequence. Human cathepsin G differs from consensus at two of three (Ala189 and Glu226) specificity triad residues (58). Mouse cathepsin G and most other mammalian proteases match consensus sequence at these residues (59).

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HOW IMMUNE PEPTIDASES CHANGE SPECIFICITY

    doi: 10.4049/jimmunol.1002292

    Figure Lengend Snippet: Aligned portions of the catalytic domains (amino acids 185–220 using standard chymotrypsinogen numbering) bracket specificity-determining “triad” residues 189, 216, and 226 (shaded). Ser195 involved in hydrolysis is marked with an asterisk. Hyphens indicate identity with human sequence. Human cathepsin G differs from consensus at two of three (Ala189 and Glu226) specificity triad residues (58). Mouse cathepsin G and most other mammalian proteases match consensus sequence at these residues (59).

    Article Snippet: Human cathepsin G (MP Biomedicals) active concentration was determined by assay with 1 mM suc-L-Val-Pro-Phe-4NA from specific activity derived from published kinetic values of active site-titrated enzyme ( 42 ).

    Techniques: Sequencing

    The graph compares hydrolytic rates using peptidyl-4NA substrates with P1 Phe, normalized for concentration of active peptidase (nM). White and black bars represent activity of human and mouse cathepsin G, respectively. All substrates were studied in PBS at 1 mM. Substrates are as follows: suc-L-Val-Pro-Phe-4NA (VPF), suc-L-Ala-Ala-Pro-Phe-4NA (AAPF), suc-L-Ala-Glu-Pro-Phe-4NA (AEPF), suc-L-Phe-Pro-Phe-4NA (FPF), acetyl-L-Arg-Glu-Thr-Phe-4NA (RETF), and benzoyl-L-Phe-4NA (F). Results represent mean ± SD of two independent experiments.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HOW IMMUNE PEPTIDASES CHANGE SPECIFICITY

    doi: 10.4049/jimmunol.1002292

    Figure Lengend Snippet: The graph compares hydrolytic rates using peptidyl-4NA substrates with P1 Phe, normalized for concentration of active peptidase (nM). White and black bars represent activity of human and mouse cathepsin G, respectively. All substrates were studied in PBS at 1 mM. Substrates are as follows: suc-L-Val-Pro-Phe-4NA (VPF), suc-L-Ala-Ala-Pro-Phe-4NA (AAPF), suc-L-Ala-Glu-Pro-Phe-4NA (AEPF), suc-L-Phe-Pro-Phe-4NA (FPF), acetyl-L-Arg-Glu-Thr-Phe-4NA (RETF), and benzoyl-L-Phe-4NA (F). Results represent mean ± SD of two independent experiments.

    Article Snippet: Human cathepsin G (MP Biomedicals) active concentration was determined by assay with 1 mM suc-L-Val-Pro-Phe-4NA from specific activity derived from published kinetic values of active site-titrated enzyme ( 42 ).

    Techniques: Concentration Assay, Activity Assay

    Comparison of kinetics of chymotryptic (suc-L-Val-Pro-Phe-4NA-hydrolyzing) activity

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HOW IMMUNE PEPTIDASES CHANGE SPECIFICITY

    doi: 10.4049/jimmunol.1002292

    Figure Lengend Snippet: Comparison of kinetics of chymotryptic (suc-L-Val-Pro-Phe-4NA-hydrolyzing) activity

    Article Snippet: Human cathepsin G (MP Biomedicals) active concentration was determined by assay with 1 mM suc-L-Val-Pro-Phe-4NA from specific activity derived from published kinetic values of active site-titrated enzyme ( 42 ).

    Techniques:

    The diagram depicts amino acids of the specificity triad lining the primary specificity pocket of cathepsin G and related serine peptidases, with examples of side chains of substrate P1 residues at the site of hydrolysis. The Ala226Glu mutation converted a chymase-like chymotryptic enzyme into a tryptic enzyme capable of hydrolyzing peptides after Lys, as shown, in part due to introduction of the negatively charged Glu side chain, which attracts the positive charge of P1 Lys ε amino group. Configurations of classic chymotryptic and tryptic peptidases plus bovine duodenase, which uses a different configuration to accommodate tryptic and chymotryptic substrates, are shown for comparison. “Tryptase” refers to mast cell β-like tryptases, rather than to human α tryptase, which has an active site blocked by a Gly216Asp mutation (60, 61).

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HOW IMMUNE PEPTIDASES CHANGE SPECIFICITY

    doi: 10.4049/jimmunol.1002292

    Figure Lengend Snippet: The diagram depicts amino acids of the specificity triad lining the primary specificity pocket of cathepsin G and related serine peptidases, with examples of side chains of substrate P1 residues at the site of hydrolysis. The Ala226Glu mutation converted a chymase-like chymotryptic enzyme into a tryptic enzyme capable of hydrolyzing peptides after Lys, as shown, in part due to introduction of the negatively charged Glu side chain, which attracts the positive charge of P1 Lys ε amino group. Configurations of classic chymotryptic and tryptic peptidases plus bovine duodenase, which uses a different configuration to accommodate tryptic and chymotryptic substrates, are shown for comparison. “Tryptase” refers to mast cell β-like tryptases, rather than to human α tryptase, which has an active site blocked by a Gly216Asp mutation (60, 61).

    Article Snippet: Human cathepsin G (MP Biomedicals) active concentration was determined by assay with 1 mM suc-L-Val-Pro-Phe-4NA from specific activity derived from published kinetic values of active site-titrated enzyme ( 42 ).

    Techniques: Mutagenesis

    Panel a contains HPLC chromatograms of angiotensin (Ang) I after incubation with human chymase, human cathepsin G, and wild type mouse cathepsin G. Peaks (as detected by monitoring absorbance at 210 nm) correspond to dipeptide HL and active octapeptide product Ang II (both resulting from hydrolysis at Phe8), inactive tetrapeptide DRVY and hexapeptide IHPFHL (resulting from hydrolysis at Tyr4), and uncleaved Ang I, as indicated. Panel b shows results of SDS-PAGE of casein after incubation with peptidases mouse cathepsin G (mCG), Ala226Glu and Ser189Ala/Ala226Glu mutants, and human cathepsin G (hCG). Size in kDa and elution positions of marker proteins are indicated.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HOW IMMUNE PEPTIDASES CHANGE SPECIFICITY

    doi: 10.4049/jimmunol.1002292

    Figure Lengend Snippet: Panel a contains HPLC chromatograms of angiotensin (Ang) I after incubation with human chymase, human cathepsin G, and wild type mouse cathepsin G. Peaks (as detected by monitoring absorbance at 210 nm) correspond to dipeptide HL and active octapeptide product Ang II (both resulting from hydrolysis at Phe8), inactive tetrapeptide DRVY and hexapeptide IHPFHL (resulting from hydrolysis at Tyr4), and uncleaved Ang I, as indicated. Panel b shows results of SDS-PAGE of casein after incubation with peptidases mouse cathepsin G (mCG), Ala226Glu and Ser189Ala/Ala226Glu mutants, and human cathepsin G (hCG). Size in kDa and elution positions of marker proteins are indicated.

    Article Snippet: Human cathepsin G (MP Biomedicals) active concentration was determined by assay with 1 mM suc-L-Val-Pro-Phe-4NA from specific activity derived from published kinetic values of active site-titrated enzyme ( 42 ).

    Techniques: Incubation, SDS Page, Marker