Suc-Val-Pro-Phe-pNA, also known as Succinyl-Valine-Proline-Phenylalanine-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical assays, particularly for the study of proteolytic enzymes. This compound features a sequence of amino acids linked by peptide bonds, with a succinyl group at the N-terminus and a p-nitroanilide moiety at the C-terminus, which serves as a chromogenic indicator. The presence of the p-nitroanilide group allows for the detection of enzymatic activity through colorimetric changes upon cleavage by specific proteases. Suc-Val-Pro-Phe-pNA is characterized by its stability under physiological conditions, making it suitable for in vitro studies. Its specificity for certain enzymes, such as serine proteases, enables researchers to investigate enzyme kinetics and mechanisms. Additionally, the compound's solubility in aqueous solutions facilitates its use in various laboratory settings. Overall, Suc-Val-Pro-Phe-pNA is a valuable tool in the field of enzymology and peptide research.

Suc-Val-Pro-Phe-pNA

95192-11-3: Suc-Val-Pro-Phe-pNA, also known as Succinyl-Valine-Proline-Phenylalanine-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical assays, particularly for the study of proteolytic enzymes. This compound features a sequence of amino acids linked by peptide bonds, with a succinyl group at the N-terminus and a p-nitroanilide moiety at the C-terminus, which serves as a chromogenic indicator. The presence of the p-nitroanilide group allows for the detection of enzymatic activity through colorimetric changes upon cleavage by specific proteases. Suc-Val-Pro-Phe-pNA is characterized by its stability under physiological conditions, making it suitable for in vitro studies. Its specificity for certain enzymes, such as serine proteases, enables researchers to investigate enzyme kinetics and mechanisms. Additionally, the compound's solubility in aqueous solutions facilitates its use in various laboratory settings. Overall, Suc-Val-Pro-Phe-pNA is a valuable tool in the field of enzymology and peptide research.

Suc-Val-Pro-Phe-pNA is an analog of the natural substrate, pNPG. It is a synthetic peptide that has been tested on neutrophils and mastocytomas for its ability to inhibit chymases. Suc-Val-Pro-Phe-pNA is hydrophobic, which means it does not dissolve in water and can therefore pass through the membrane and into the cytoplasm of cells. This peptide also interacts with soybean trypsin inhibitor, which inhibits proteolytic enzymes, such as chymases.

<p>Suc-VPF-pNA, sensitive substrate for mammalian chymotrypsin and chymotrypsin-like enzymes, such as human leukocyte cathepsin G, human and dog skin chymases, and rat mast cell proteases.</p>

CAS 95192-11-3

Suc-Val-Pro-Phe-pNA

Suc-Val-Pro-Phe-pNA

Ref: 3D-FS110779

Suc-Val-Pro-Phe-pNA

Ref: 01-4018017