Ac-Met-AMC

Ac-Met-AMC is an acetylated methionine amino acid-AMC (7-amino-4-methylcoumarin) substrate construct designed for enzyme activity and substrate specificity studies where fluorescence readout is used to monitor cleavage. The AMC reporting group provides a convenient signal upon enzymatic release, making this reagent a practical tool for screening protease or peptidase activity in biochemical assays and for comparing relative catalytic behavior across conditions and substrate variants.

1. Enzyme Activity Fluorescence

Ac-Met-AMC is used as a fluorogenic substrate in enzymatic assays to quantify protease or peptidase activity through the generation of the AMC fluorescent product. Researchers in biochemistry and chemical biology typically employ this type of substrate to obtain kinetic readouts (e.g., initial rates) and to benchmark how assay conditions, inhibitors, or buffer compositions influence catalytic turnover, leveraging the strong fluorescence signal associated with AMC release.

2. Protease Specificity Screening

Ac-Met-AMC supports substrate profiling workflows in which a panel of amino acid-AMC derivatives is compared to determine relative preferences for methionine-containing motifs and to map cleavage behavior across enzyme families. In inhibitor discovery and mechanistic studies, this construct is often selected as a defined, small-molecule substrate that reduces ambiguity from heterogeneous protein substrates, enabling clearer interpretation of specificity trends and assay-to-assay comparability.

3. Cleavage Assay Development

Ac-Met-AMC is commonly incorporated into assay development and method optimization efforts for fluorescent protease testing, including establishing practical assay windows, signal-to-background behavior, and readout conditions compatible with plate-based measurements. Analytical and R&D teams use the defined acetylated methionine-AMC format to streamline evaluation of reaction parameters such as incubation time, enzyme concentration ranges, and quench/stop strategies, facilitating reproducible downstream comparisons in screening or characterization experiments.

4. Proteomics-Adjacent Substrate Studies

Ac-Met-AMC is also used in proteomics-adjacent studies where small, defined substrates help validate or complement observations from peptide-based experiments, such as assessing whether an enzyme preparation exhibits activity toward methionine-terminating or methionine-centered cleavage patterns. Chemical biology groups often use this construct to connect enzymatic behavior seen in more complex peptide contexts to simpler, controlled substrate systems, supporting rational selection of peptide substrates for subsequent LC-MS or fluorescence-based characterization.

1. Sex differences in oxidative stress level and antioxidative enzymes expression and activity in obese pre-diabetic elderly rats treated with metformin or liraglutide

2. Effect of Probiotic Lactobacillus plantarum on Streptococcus mutans and Candida albicans Clinical Isolates from Children with Early Childhood Caries

3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate

4. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

5. Application of human liver organoids as a patient-derived primary model for HBV infection and related hepatocellular carcinoma