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New In-Stock Product | H-β-Ala-AMC ∙ TFA (CAS: 201847-54-3): A Fluorescent “Switch-On” Substrate Specifically Designed for β-Aminopeptidase Activity Assays
2026/3/25 13:13:15 Browse volume(4)H-β-Ala-AMC∙TFA (CAS: 201847-54-3)
In the toolbox of enzymology research, α-amino acid-AMC substrates are almost a standard kit — Leu-AMC for leucine aminopeptidase, Arg-AMC for arginine aminopeptidase, with a wide range of models and mature protocols.
However, when the research focus shifts to β-aminopeptidases — such as the hydrolysis activity of carnosinase on β-alanyl peptide bonds, or when the goal is to "isolate" the β-aminopeptidase signal from the α-aminopeptidase background in a mixed enzyme system — the choice of suitable fluorescent substrates narrows drastically. Substitute with α-Ala-AMC? The enzyme won't recognize it. Switch to the colorimetric substrate β-Ala-pNA? Its sensitivity often falls short of the threshold needed for low-abundance samples.
H-β-Ala-AMC ∙ TFA is a fluorescent substrate designed precisely to fill this gap. It uses β-alanine as the enzyme recognition element and AMC as the fluorescence switch, combining β-amino acid selectivity with fluorescence-level sensitivity, making "detectability" and "discriminability" no longer mutually exclusive.
Chinese Name: β-Alanine 7-amido-4-methylcoumarin trifluoroacetate
English Name: H-β-Ala-AMC ∙ TFA
Abbreviation: β-Alanine 7-amido-4-methylcoumarin trifluoroacetate
CAS Number: 201847-54-3
Molecular Formula: C15H15F3N2O5
Molecular Weight: 360.29
Specifications: 1 g / 5 g / 25 g (Custom packaging supported)
Form: Lyophilized powder
Product Number: G04050017
Stock: In stock
Luminescence: Blue fluorescence
The working mechanism of H-β-Ala-AMC ∙ TFA follows a classic "structure-event-signal" logic chain. In the unreacted state, the AMC fluorophore is tightly linked to β-alanine via an amide bond, locking the molecule's fluorescence properties. When a sample containing the specific aminopeptidase is introduced into the system, the enzyme precisely recognizes the β-alanine residue and acts like a pair of molecular scissors, cleaving the amide bond. This cleavage event instantly releases free AMC molecules, which then emit a strong blue fluorescence signal under UV excitation. The signal intensity is proportional to the enzyme activity and can be read continuously in real-time using a fluorescence microplate reader.
• Quantitative Detection of Aminopeptidase Activity
Utilizing its high fluorescence quantum yield for micro-kinetic analysis of samples containing specific aminopeptidases (such as those targeting β-alanine sequences) in in vitro biochemical experiments.
• Inhibitor Screening and Drug Development
Suitable for high-throughput screening systems to rapidly evaluate the inhibitory effects of candidate molecules on aminopeptidases.
• Rapid Microbial Phenotypic Identification
Because some pathogenic bacteria or specific cell lines possess unique enzymatic characteristics for degrading β-alanine substrates, this product can be integrated into culture media as a core chromogenic/luminescent raw material.
✅ Sensitive Signal
Strong fluorescence response upon AMC release, enabling detection of low-abundance enzyme activity and lowering the detection limit.
✅ Real-Time Readout
Fluorescence signal changes continuously with the reaction ; obtain kinetic curves directly without stopping the reaction.
✅ Low Background
Extremely weak fluorescence in the unhydrolyzed state , significantly improves signal-to-noise ratio for clearer, more reliable data.
✅ Three In-Stock Sizes
One-stop solution from development to scale-up: 1 g suitable for methodology exploration, 5 g for medium-scale validation, 25 g covering large projects or pilot-scale needs. Three specifications available from stock, with custom packaging also open — ensuring no delays caused by supply lead times.
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