Pglu-arg-thr-lys-arg 7-amido-4-methylcoumarin, commonly referred to as a peptide substrate, is characterized by its structure, which includes a sequence of amino acids (proline, arginine, threonine, lysine, and arginine) linked to a 7-amido-4-methylcoumarin moiety. This compound is often utilized in biochemical assays, particularly for studying proteolytic enzymes due to its fluorescent properties. The 7-amido-4-methylcoumarin group serves as a fluorogenic tag, allowing for the detection of enzymatic activity through fluorescence upon cleavage by specific proteases. The peptide sequence can be tailored to target particular enzymes, making it a versatile tool in research. Additionally, the compound's solubility and stability in aqueous solutions are important for its application in biological systems. Overall, Pglu-arg-thr-lys-arg 7-amido-4-methylcoumarin is significant in the field of biochemistry for its role in enzyme activity assays and its potential applications in drug discovery and development.

pglu-arg-thr-lys-arg 7-amido-4-*methylcoumarin

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L-Argininamide, 5-oxo-L-prolyl-L-arginyl-L-threonyl-L-lysyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-

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Pyr-Arg-Thr-Lys-Arg-AMC trifluoroacetate salt

The fluorogenic substrate pERTKR-AMC is efficiently cleaved by furin, a mammalian homolog of the yeast Kex2 endoprotease (kcat/Km approx. 2·10⁴ M-¹s-¹). As a calcium-dependent serine protease associated with Golgi membranes, furin is responsible for the secretory processing of precursor proteins at paired basic residues. Also cleaved by proprotein convertase 4. Pyr-RTKR-AMC is an excellent substrate for flavivirin.

CAS 155575-02-3: pglu-arg-thr-lys-arg 7-amido-4-*methylcoumarin

L-Argininamide, 5-oxo-L-prolyl-L-arginyl-L-threonyl-L-lysyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-

Ref: IN-DA001NZR

Pyr-Arg-Thr-Lys-Arg-AMC trifluoroacetate salt

Ref: 3D-FP110566

Pyr-Arg-Thr-Lys-Arg-AMC

Ref: 01-4018149

Pyr-Arg-Thr-Lys-Arg-MCA

Ref: 3D-MPR-3159-V