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fluorogenic substrate meosuc-ala-ala-pro-val-amc  (Bachem)

 
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    Bachem fluorogenic substrate meosuc-ala-ala-pro-val-amc
    Fluorogenic Substrate Meosuc Ala Ala Pro Val Amc, supplied by Bachem, 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/pro+fluorogenic+substrate/fluorogenic+substrate+meosuc+ala+ala+pro+val+amc/us09440930-402-8-11
    Average 90 stars, based on 1 article reviews
    fluorogenic substrate meosuc-ala-ala-pro-val-amc - by Bioz Stars, 2026-09
    90/100 stars

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    other:

    Article Title: Machine-learning algorithms define pathogen-specific local immune fingerprints in peritoneal dialysis patients with bacterial infections
    Article Snippet: Active human neutrophil elastase was measured using the fluorogenic substrate MeOSuc-Ala-Ala-Pro-Val-AMC (Bachem, Bubendorf, Switzerland); active MMP was measured using the fluorogenic substrate Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH 2 (Enzo Life Sciences, Farmingdale, NY) and by zymography using precast Novex gelatin zymogram gels (Invitrogen) scanned on a Bio-Rad GS800 densitometer (Bio-Rad Laboratories, Berkeley, CA) and analyzed using ImageJ software.

    Article Title: Comparison of Fucoidans from Saccharina latissima Regarding Age-Related Macular Degeneration Relevant Pathomechanisms in Retinal Pigment Epithelium
    Article Snippet: Elastase inhibitory activity of the fucoidans was examined by a fluorogenic microplate assay (nuncTM 237108, Thermo Fisher Scientific, Waltham, MA, USA) using elastase from human polymorph nuclear granulocytes (PMN) (art.-No. 324681; Merck Chemicals GmbH, Darmstadt, Germany) and the substrate I-1270 (MeOSuc-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin; Bachem AG, Bubendorf, Switzerland).

    Article Title: Comparison of Fucoidans from Saccharina latissima Regarding Age-Related Macular Degeneration Relevant Pathomechanisms in Retinal Pigment Epithelium.
    Article Snippet: Elastase inhibitory activity of the fucoidans was examined by a fluorogenic microplate assay (nuncTM 237108, Thermo Fisher Scientific, Waltham, MA, USA) using elastase from human polymorph nuclear granulocytes (PMN) (art.-No. 324681; Merck Chemicals GmbH, Darmstadt, Germany) and the substrate I-1270 (MeOSuc-Ala-Ala-Pro-Val-7-amido4-methylcoumarin; Bachem AG, Bubendorf, Switzerland).

    Article Title: Substituted spirocycles
    Article Snippet: Neutrophile Elastase (NE) Measurement: NE activity in the BALF (bronchioalveolar lavage fluid) cell lysate was measured using the fluorescent NE substrate MeOSuc-Ala-Ala-Pro-Val-AMC (Bachem): 10 μl cell lysate were mixed with 5 μl assay buffer (20 mM Tris pH 7.5, 100 mM NaCl, 0.1% human serum albumin) and 5 μl substrate (1 mM in assay buffer) in a 384 well plate (Optiplate 384f, PerkinElmer).

    Article Title: Substituted bicyclic dihydropyrimidinones and their use as inhibitors of neutrophil elastase activity
    Article Snippet: Subsequently, the enzyme activity is measured using the fluorogenic substrate MeOSuc-Ala-Ala-Pro-Val-AMC (Bachem Cat. No. 1-1270, substrate concentration: 250 μM, pH 7.5, 25 mM TRIS buffer, 250 mM NaCl) in analogous fashion as described for the human neutrophil assay.

    Article Title: Fluorescent diphenylphosphonate-based probes for detection of serine protease activity during inflammation
    Article Snippet: Alternatively, elastase activity was measured with the fluorogenic substrate probe MeOSucc-Ala-Ala-Pro-Val-7-amino-4-methylcoumarin (Bachem, AAPV-AMC).

    Article Title: Substituted bicyclic dihydropyrimidinones and their use as inhibitors of neutrophil elastase activity
    Article Snippet: Subsequently, the enzyme activity is measured using the fluorogenic substrate MeOSuc-Ala-Ala-Pro-Val-AMC (Bachem Cat. No. I-1270, substrate concentration: 250 μM, pH 7.5, 25 mM TRIS buffer, 250 mM NaCl) in analogous fashion as described for the human neutrophil assay.

    Activity Assay:

    Article Title: Wound prognosis
    Article Snippet: .. Determining the Amount of Elastase by Fluorogenic Activity Assay A fluorogenic substrate, MeOSuc-Ala-Ala-Pro-Val-AMC (BaChem) (SEQ ID NO: 7) which is cleaved by elastase to release the fluorogenic group 7-amino-4-methylcoumarin was used to measure elastase activity in the wound fluid samples. ..



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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 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