Z-Ala-Pro-pNA, also known as Z-Ala-Pro-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical research, particularly in studies involving proteases. The "Z" in its name indicates that it is a protected form of the amino acid alanine (Ala), where the N-terminal amine is acetylated or benzyloxycarbonyl (Z) protected to enhance stability and solubility. The proline (Pro) residue contributes to the peptide's structural properties, influencing its conformation and interaction with enzymes. The p-nitroanilide (pNA) moiety serves as a chromogenic group, allowing for the quantification of enzymatic activity through colorimetric assays. Upon cleavage by specific proteases, Z-Ala-Pro-pNA releases p-nitroaniline, which can be measured spectrophotometrically. This compound is valuable in enzyme kinetics studies and the development of protease inhibitors. Its stability, solubility, and the ability to provide a measurable product upon enzymatic action make it a useful tool in both academic and pharmaceutical research settings.

Z-Ala-Pro-pNA

66382-56-7: Z-Ala-Pro-pNA, also known as Z-Ala-Pro-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical research, particularly in studies involving proteases. The "Z" in its name indicates that it is a protected form of the amino acid alanine (Ala), where the N-terminal amine is acetylated or benzyloxycarbonyl (Z) protected to enhance stability and solubility. The proline (Pro) residue contributes to the peptide's structural properties, influencing its conformation and interaction with enzymes. The p-nitroanilide (pNA) moiety serves as a chromogenic group, allowing for the quantification of enzymatic activity through colorimetric assays. Upon cleavage by specific proteases, Z-Ala-Pro-pNA releases p-nitroaniline, which can be measured spectrophotometrically. This compound is valuable in enzyme kinetics studies and the development of protease inhibitors. Its stability, solubility, and the ability to provide a measurable product upon enzymatic action make it a useful tool in both academic and pharmaceutical research settings.

The prolyl oligopeptidase (POP) substrate Z-AP-pNA was used in combination with Z-GP-pNA and Z-AA-pNA for characterizing the prolyl oligopeptide of of the hyperthermophile Pyrococcus furiosus.

Z-Ala-Pro-pNA is a serine protease that cleaves peptide bonds in proteins. It has been shown to be active against a number of organisms, including Pyrococcus furiosus and Porcine pancreatic extracts, as well as specificities such as amino acid residues and oligopeptidases. Z-Ala-Pro-pNA may have uses in the food industry by acting on proteins that are found in meat products.

CAS 66382-56-7

Z-Ala-Pro-pNA

Z-Ala-Pro-pNA

Ref: 01-4003575

Z-Ala-Pro-pNA

Ref: 3D-FA110716