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fluorogenic tripeptide substrate h met gly proamc  (R&D Systems)


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    R&D Systems fluorogenic tripeptide substrate h met gly proamc
    Fluorogenic Tripeptide Substrate H Met Gly Proamc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/H-Met-Gly-Pro-AMC+Fluorogenic+Peptide+Substrate/pm41239757-64-10-18
    Average 94 stars, based on 32 article reviews
    fluorogenic tripeptide substrate h met gly proamc - by Bioz Stars, 2026-11
    94/100 stars

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    Related Articles

    Activation Assay:

    Article Title: The hills are alive with the sound of venom: Clinical implications of intraspecific variations in Factor Va mediated activations of Factor VII and Factor X in Swiss populations of Vipera aspis (Asp Viper).
    Article Snippet: .. Cross-contamination between runs was prevented by cleaning the Fluoroskan interior with 95% ethanol, followed by 100% ddH 2 O, and finally priming with the reaction substrate solution containing Fluorogenic Peptide Substrate ES011 (Boc-Val-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) diluted in 5 mM CaCl 2 + OK buffer in a 500:1 ratio (250:1 for prothrombin activation). ..

    Article Title: Hemostatic hellfire: Rhabdophis helleri (Red-necked Keelback) snake venom pathophysiologically activates Factor VII and Factor X through novel uses of the clotting cofactors calcium, phospholipid, and Factor Va.
    Article Snippet: .. Cross-contamination between runs was prevented by cleaning the Fluoroskan interior with 95 % ethanol, followed by 100 % ddH2O, and finally priming with the reaction substrate solution containing Fluorogenic Peptide Substrate ES011 (BocVal-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) diluted in 5 mM CaCl2 + OK buffer in a 500:1 ratio (250:1 for prothrombin activation). ..

    Article Title: The shifting sands of venom: Divergent blood clotting factor activation pathways and differential Factor Va co-factor dependence for the venoms of Middle Eastern desert vipers (Eristicophis and Pseudocerastes species).
    Article Snippet: .. Crosscontamination between runs was prevented by cleaning the Fluoroskan interior with 95 % ethanol, followed by 100 % ddH2O, and finally priming with the reaction substrate solution containing Fluorogenic Peptide Substrate ES011 (Boc-Val-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) diluted in 5 mM CaCl2 + OK buffer in a 500:1 ratio (250:1 for prothrombin activation). ..

    other:

    Article Title: Hemostatic hellfire: Rhabdophis helleri (Red-necked Keelback) snake venom pathophysiologically activates Factor VII and Factor X through novel uses of the clotting cofactors calcium, phospholipid, and Factor Va.
    Article Snippet: Therefore, the solution for these experimental conditions contained Fluorogenic Peptide Substrate ES011 (Boc-Val-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) diluted in 5 mM OK Buffer.

    Incubation:

    Article Title: The sting that clots: The Factor VII and Factor X activating procoagulant effects of Androctonus scorpion venoms are potentiated by Factor Va as a cofactor.
    Article Snippet: .. To obtain uniform mixing, plates were shaken for 3s before each measurement while being incubated at 37 ◦ C. Fluorescence generated by enzymatic cleavage of the fluorogenic Peptide Substrate ES011 (Boc-Val-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) were measured for 150 readings using excitation and emission wavelengths of 390 nm and 460 nm, respectively. ..

    Fluorescence:

    Article Title: The sting that clots: The Factor VII and Factor X activating procoagulant effects of Androctonus scorpion venoms are potentiated by Factor Va as a cofactor.
    Article Snippet: .. To obtain uniform mixing, plates were shaken for 3s before each measurement while being incubated at 37 ◦ C. Fluorescence generated by enzymatic cleavage of the fluorogenic Peptide Substrate ES011 (Boc-Val-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) were measured for 150 readings using excitation and emission wavelengths of 390 nm and 460 nm, respectively. ..

    Generated:

    Article Title: The sting that clots: The Factor VII and Factor X activating procoagulant effects of Androctonus scorpion venoms are potentiated by Factor Va as a cofactor.
    Article Snippet: .. To obtain uniform mixing, plates were shaken for 3s before each measurement while being incubated at 37 ◦ C. Fluorescence generated by enzymatic cleavage of the fluorogenic Peptide Substrate ES011 (Boc-Val-Pro-Arg-AMC; R&D Systems, catalog #ES011, Minneapolis, MN, USA) were measured for 150 readings using excitation and emission wavelengths of 390 nm and 460 nm, respectively. ..



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    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.
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    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.
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    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.
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    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.
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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