CAS 191723-64-5: L-histidine 7-amindo-4-methylcoumarin

L-Histidine 7-amido-4-methylcoumarin hydrochloride is a synthetic peptide substrate used as a fluorogenic substrate for histidine aminopeptidase.

L-Histidine 7-amido-4-methylcoumarin hydrochloride is a fluorogenic substrate, which is a synthetic chemical that is used as a substitute for natural substrates. It reacts with enzymes in the presence of hydrogen peroxide to produce light. This product has been used as an enzyme substrate, a diagnostic tool and has been used to detect bacterial growth in culture media. L-Histidine 7-amido-4-methylcoumarin hydrochloride is also used for food testing and environmental testing, where it can be used as a chromogenic substrate or conjugate respectively. This product has CAS number 5981-00-6 and molecular weight of 254.27 g/mol.

L-Histidine 7-amido-4-methylcoumarin is a versatile building block that is useful in the synthesis of complex compounds. It can be used as a reaction component or scaffold to form new chemical entities with desired properties. L-Histidine 7-amido-4-methylcoumarin has been utilized as a reagent, speciality chemical, and research chemical for over 50 years. The compound has high purity and quality, and offers an excellent price point for research purposes.

Bachem ID: 4015210.

L-Histidine 7-amido-4-methylcoumarin is a proteolytic enzyme that cleaves proteins at the N-terminal amino acid residue. It was originally purified from a bacterial expression plasmid, but has since been found in other bacteria. The gene product of this enzyme has also been found in bacteriophages and some strains of Proteus mirabilis and Escherichia coli. The biochemical activity of L-Histidine 7-amido-4-methylcoumarin is similar to that of subtilisin, which consists of hydrolyzing peptide bonds with a pK at around 10.5. Spectrometry analysis has shown that L-Histidine 7-amido-4-methylcoumarin is an acidic protein with an optimum pH for activity around 2.2. Hydroxyapatite, polymerase chain reaction (PCR), and cloning experiments have shown that this enzyme may be involved