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fluorogenic pop substrate suc gly pro leu gly pro 7 amido 4methylcoumarin amc  (Thermo Fisher)


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    Structured Review

    Thermo Fisher fluorogenic pop substrate suc gly pro leu gly pro 7 amido 4methylcoumarin amc
    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, 2026-11
    97/100 stars

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    Article Title: Single Layer Centrifugation Improves the Quality of Fresh Donkey Semen and Modifies the Sperm Ability to Interact with Polymorphonuclear Neutrophils
    Article Snippet: Lipid disorder of plasma membrane was evaluated following the protocol set by Rathi et al. [ ] with minor modifications [ ], which is based on M540 and YO-PRO-1 fluorochromes (Molecular Probes, ThermoFisher Scientific).

    Article Title: A Vascular Graft On‐a‐Chip Platform for Assessing the Thrombogenicity of Vascular Prosthesis and Coatings with Tuneable Flow and Surface Conditions
    Article Snippet: 2022, 32, 2205078 fluorogenic substrate Boc-Val-Pro-Arg-7-AMC was purchased from Thermo Fisher Scientific (Massachusetts, United States). ePTFE vascular grafts were purchased from Gore (Toronto, Ontario, Canada).PMMA, nylon, PE, PVC, and silicone were obtained from online distributors.

    Article Title: The novel piperine derivative MHJ-LN inhibits breast cancer by inducing apoptosis via p53 activation.
    Article Snippet: Triple-negative breast cancer (TNBC) is characterized by high aggressiveness and recurrence rates due to the lack of effective treatment options.. Piperine, a natural alkaloid extracted from black pepper, has demonstrated significant anticancer potential in recent years.. Therefore, developing piperine derivatives to enhance its anticancer effects holds critical clinical significance.

    Article Title: Rational design of anti-GITR-based combination immunotherapy
    Article Snippet: Caspase activation assays were performed by incubating CD8 + , CD4 + CD25 − Teff and CD4 + CD25 hi Tregs immunomagnetically purified (human CD4 + CD25 + Regulatory T Cell Isolation kit, Miltenyi Biotec) from healthy donor PBMC samples with plate-bound anti-CD3 (1 μg/ml), TRX518 or isotype control or recombinant human GITR ligand (GenScript) (10 μg/ml) and soluble anti-CD28 (0.1 μg/ml) in the presence of a fluorogenic caspase 3/7 substrate (1μM, Invitrogen) for 16 and 32 hours.

    Activity Assay:

    Article Title: Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP.
    Article Snippet: .. Fluorogenic POP substrate Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4methylcoumarin (AMC) (HANGZHOU JHECHEM CO LTD) was diluted in PBS to 1–25 μMfinal concentrations in96-well plates (ThermoFisher) to measure enzyme activity parameters in real time, with end-point reactions at 10 and 30min, using a Gen5TM Microplate Reader and Imager Software. ..

    Article Title: Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP
    Article Snippet: .. Fluorogenic POP substrate Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin (AMC) (HANGZHOU JHECHEM CO LTD) was diluted in PBS to 1–25 μM final concentrations in 96-well plates (ThermoFisher) to measure enzyme activity parameters in real time, with end-point reactions at 10 and 30 min, using a Gen5TM Microplate Reader and Imager Software. ..

    Software:

    Article Title: Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP.
    Article Snippet: .. Fluorogenic POP substrate Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4methylcoumarin (AMC) (HANGZHOU JHECHEM CO LTD) was diluted in PBS to 1–25 μMfinal concentrations in96-well plates (ThermoFisher) to measure enzyme activity parameters in real time, with end-point reactions at 10 and 30min, using a Gen5TM Microplate Reader and Imager Software. ..

    Article Title: Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP
    Article Snippet: .. Fluorogenic POP substrate Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin (AMC) (HANGZHOU JHECHEM CO LTD) was diluted in PBS to 1–25 μM final concentrations in 96-well plates (ThermoFisher) to measure enzyme activity parameters in real time, with end-point reactions at 10 and 30 min, using a Gen5TM Microplate Reader and Imager Software. ..

    Cleavage Assay:

    Article Title: Platelets inhibit apoptotic lung epithelial cell death and protect mice against infection-induced lung injury
    Article Snippet: Time-lapse large-area images (5 × 5 fields) were collected every 15 minutes using a 20× dry optic (0.75 numerical aperture) and stitched using NIS Elements (Nikon). .. Flow cytometric–based caspase-3/7 cleavage assay After experimental exposure, MLE 12 cells were incubated with a fluorogenic caspase-3/7 substrate ( {"type":"entrez-nucleotide","attrs":{"text":"C10740","term_id":"1535811","term_text":"C10740"}} C10740 , Invitrogen) per the manufacturer’s instructions. .. Flow cytometry was performed immediately on a FACSCalibur machine (BD Biosciences) and analyzed with FlowJo V10.

    Incubation:

    Article Title: Platelets inhibit apoptotic lung epithelial cell death and protect mice against infection-induced lung injury
    Article Snippet: Time-lapse large-area images (5 × 5 fields) were collected every 15 minutes using a 20× dry optic (0.75 numerical aperture) and stitched using NIS Elements (Nikon). .. Flow cytometric–based caspase-3/7 cleavage assay After experimental exposure, MLE 12 cells were incubated with a fluorogenic caspase-3/7 substrate ( {"type":"entrez-nucleotide","attrs":{"text":"C10740","term_id":"1535811","term_text":"C10740"}} C10740 , Invitrogen) per the manufacturer’s instructions. .. Flow cytometry was performed immediately on a FACSCalibur machine (BD Biosciences) and analyzed with FlowJo V10.



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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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    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.
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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