fluorogenic substrate gly-pro-amc Search Results


fluorogenic tripeptide substrate h met gly pro amc  (R&D Systems)
93
R&D Systems fluorogenic tripeptide substrate h met gly pro amc
Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
Fluorogenic Tripeptide Substrate H Met Gly Pro Amc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fluorogenic tripeptide substrate methionine glycine proline 7 amido methylcoumarin  (R&D Systems)
92
R&D Systems fluorogenic tripeptide substrate methionine glycine proline 7 amido methylcoumarin
Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
Fluorogenic Tripeptide Substrate Methionine Glycine Proline 7 Amido Methylcoumarin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 1 article reviews
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fluorogenic peptides vgr-amc  (Biomol GmbH)
90
Biomol GmbH fluorogenic peptides vgr-amc
Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
Fluorogenic Peptides Vgr Amc, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fluorogenic peptide substrates tryptase “tos-gly-pro-lys-amc  (DSM NV Inc)
90
DSM NV Inc fluorogenic peptide substrates tryptase “tos-gly-pro-lys-amc
Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
Fluorogenic Peptide Substrates Tryptase “Tos Gly Pro Lys Amc, supplied by DSM NV Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fluorogenic peptide substrates tryptase “tos-gly-pro-lys-amc - by Bioz Stars, 2026-08
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fluorogenic substrate gly-pro-aminomethylcoumarin (amc)  (Cayman Chemical)
90
Cayman Chemical fluorogenic substrate gly-pro-aminomethylcoumarin (amc)
Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
Fluorogenic Substrate Gly Pro Aminomethylcoumarin (Amc), supplied by Cayman Chemical, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the fluorogenic tripeptide substrate H‐Met‐Gly‐Pro‐AMC was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.

Journal: Febs Letters

Article Title: The Caenorhabditis elegans DPF ‐3 and human DPP4 have tripeptidyl peptidase activity

doi: 10.1002/1873-3468.70219

Figure Lengend Snippet: Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the fluorogenic tripeptide substrate H‐Met‐Gly‐Pro‐AMC was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.

Article Snippet: Enzymatic activities of hDPP4 and DPF‐3 were measured using the fluorogenic tripeptide substrate H‐Met‐Gly‐Pro‐AMC (7‐amino‐4‐methylcoumarin, Catalog number: ES017, R&D Systems).

Techniques: Activity Assay, Mutagenesis, Concentration Assay, Fluorescence, Generated, Standard Deviation