Review



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


Bioz Verified Symbol R&D Systems is a verified supplier
Bioz Manufacturer Symbol R&D Systems manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 94
      Buy from Supplier

    Structured Review

    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, 2026-10
    94/100 stars

    Images

    Related Articles

    Cleavage Assay:

    Article Title: Cryo-EM reveals that iRhom2 restrains ADAM17 protease activity to control the release of growth factor and inflammatory signals
    Article Snippet: .. Peptide substrate cleavage assay The protease activity of the purified ADAM17 complex was measured using a fluorogenic peptide substrate Mca-PLAQAV-DpaRSSSR-NH2 (R&D Systems, catalog #ES003) (Figures S5A and S5B). ..

    Activity Assay:

    Article Title: Cryo-EM reveals that iRhom2 restrains ADAM17 protease activity to control the release of growth factor and inflammatory signals
    Article Snippet: .. Peptide substrate cleavage assay The protease activity of the purified ADAM17 complex was measured using a fluorogenic peptide substrate Mca-PLAQAV-DpaRSSSR-NH2 (R&D Systems, catalog #ES003) (Figures S5A and S5B). ..

    Article Title: Tyrosine nitration moderates the peptidase activity of human methionyl aminopeptidase 2.
    Article Snippet: Methionyl aminopeptidase 2 (MetAP2) plays an important role in the regulation of angiogenesis.. This study examined whether nitration of MetAP2 alters its enzymatic activity in vitro.. The activity of unmodified, nitrated and oxidised MetAP2 was assessed and it was found that nitration significantly reduced its ability to cleave a chromogenic substrate.

    Purification:

    Article Title: Cryo-EM reveals that iRhom2 restrains ADAM17 protease activity to control the release of growth factor and inflammatory signals
    Article Snippet: .. Peptide substrate cleavage assay The protease activity of the purified ADAM17 complex was measured using a fluorogenic peptide substrate Mca-PLAQAV-DpaRSSSR-NH2 (R&D Systems, catalog #ES003) (Figures S5A and S5B). ..

    Recombinant:

    Article Title: Discovery of Inhibitors of Burkholderia pseudomallei Methionine Aminopeptidase with Antibacterial Activity
    Article Snippet: .. The fluorogenic peptide substrate, H-Met-Gly-Pro-7-amino-4-methylcoumarin hydrochloride (H-metGly-Pro-AMC), and recombinant human DPPIV/CD26 (rhDPPIV) were purchased from R&D Systems, Inc. (Minneapolis, MN). ..



    Similar Products

    fluorogenic substrate z fr afc  (MedChemExpress)
    94
    MedChemExpress fluorogenic substrate z fr afc
    Fluorogenic Substrate Z Fr Afc, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/Z-Gly-Pro-Arg-AMC+hydrochloride/pmc13399510-89-18-23
    Average 94 stars, based on 1 article reviews
    fluorogenic substrate z fr afc - by Bioz Stars, 2026-10
    94/100 stars
    		  Buy from Supplier
    fluorogenic substrate mca ala pro lys dnp oh  (MedChemExpress)
    93
    MedChemExpress fluorogenic substrate mca ala pro lys dnp oh
    Fluorogenic Substrate Mca Ala Pro Lys Dnp Oh, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/Mca-Ala-Pro-Lys(Dnp)-OH/pmc13071878-405-14-18
    Average 93 stars, based on 1 article reviews
    fluorogenic substrate mca ala pro lys dnp oh - by Bioz Stars, 2026-10
    93/100 stars
    		  Buy from Supplier
    fluorogenic substrate mcaala pro lys dnp oh  (MedChemExpress)
    93
    MedChemExpress fluorogenic substrate mcaala pro lys dnp oh
    Fluorogenic Substrate Mcaala Pro Lys Dnp Oh, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/Mca-Ala-Pro-Lys(Dnp)-OH/pm41875055-415-14-17
    Average 93 stars, based on 1 article reviews
    fluorogenic substrate mcaala pro lys dnp oh - by Bioz Stars, 2026-10
    93/100 stars
    		  Buy from Supplier
    fluorogenic tripeptide substrate h met gly proamc  (R&D Systems)
    94
    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 1 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 1 article reviews
    fluorogenic tripeptide substrate h met gly proamc - by Bioz Stars, 2026-10
    94/100 stars
    		  Buy from Supplier
    fluorogenic tripeptide substrate h met gly pro amc  (R&D Systems)
    94
    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: 94/100, based on 1 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/pmc12883895-58-10-18
    Average 94 stars, based on 1 article reviews
    fluorogenic tripeptide substrate h met gly pro amc - by Bioz Stars, 2026-10
    94/100 stars
    		  Buy from Supplier
    fluorogenic peptide substrate mca lys pro leu gly leu dap dnp ala arg nh2  (Ambeed Inc)
    86
    Ambeed Inc fluorogenic peptide substrate mca lys pro leu gly leu dap dnp ala arg nh2
    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 Substrate Mca Lys Pro Leu Gly Leu Dap Dnp Ala Arg Nh2, supplied by Ambeed Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/ala+arg+dap+dnp+fluorogenic+gly+leu+leu+lys+mca+nh2+peptide+pro+substrate/pm41101741-55-8-19
    Average 86 stars, based on 1 article reviews
    fluorogenic peptide substrate mca lys pro leu gly leu dap dnp ala arg nh2 - by Bioz Stars, 2026-10
    86/100 stars
    		  Buy from Supplier
    h met gly pro 7 amino 4 methylcoumarin hydrochloride  (R&D Systems)
    94
    R&D Systems h met gly pro 7 amino 4 methylcoumarin hydrochloride
    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.
    H Met Gly Pro 7 Amino 4 Methylcoumarin Hydrochloride, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 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/pm24376907__ml400034m_si_001-17-4-15
    Average 94 stars, based on 1 article reviews
    h met gly pro 7 amino 4 methylcoumarin hydrochloride - by Bioz Stars, 2026-10
    94/100 stars
    		  Buy from Supplier
    methoxycoumarin 4 yl acetyl pro leu gly leu  (R&D Systems)
    93
    R&D Systems methoxycoumarin 4 yl acetyl pro leu gly leu
    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.
    Methoxycoumarin 4 Yl Acetyl Pro Leu Gly Leu, 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
    https://www.bioz.com/product/pro+fluorogenic+substrate/Mca-PLGL-Dpa-AR-NH2+Fluorogenic+MMP+Substrate/us12421321-1652-22-26
    Average 93 stars, based on 1 article reviews
    methoxycoumarin 4 yl acetyl pro leu gly leu - by Bioz Stars, 2026-10
    93/100 stars
    		  Buy from Supplier
    fluorogenic pop substrate suc gly pro leu gly pro 7 amido 4methylcoumarin amc  (Thermo Fisher)
    97
    Thermo Fisher fluorogenic pop substrate suc gly pro leu gly pro 7 amido 4methylcoumarin 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 Pop Substrate Suc Gly Pro Leu Gly Pro 7 Amido 4methylcoumarin Amc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/Leupeptin+hemisulfate/pm40764299-277-0-19
    Average 97 stars, based on 1 article reviews
    fluorogenic pop substrate suc gly pro leu gly pro 7 amido 4methylcoumarin amc - by Bioz Stars, 2026-10
    97/100 stars
    		  Buy from Supplier

    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