N-Benzoyl-Phe-Val-Arg-p-nitroanilide is a chromogenic protease substrate.[1]
Application
N
-Benzoyl-Phe-Val-Arg-p-nitroanilide hydrochloride has been used: as a substrate: for trypsin-like enzyme in the soluble and particulate fractions of the hyphae[2]
for the thrombin, recombinant and native batroxobin from snake venom[3]
for fibrinolytic enzyme aprE2 in amidolytic activity assay[4]
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Chromogenic peptide substrates were developed more than 30 years ago. Although the use of chromogenic substrate methods in coagulation and fibrinolysis diagnostics was not as rapidly implemented as initially believed, they are now well established for several analytes such as
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 152(1), 54-59 (2008-10-14)
The production of enzymes and the colonization of leaves by Leucoagaricus gongylophorus were investigated to further understand the digestive interactions of leaf-cutting ant colonies. The enzymes detected were indicative of a saprophytic origin of this fungus, producing all the enzymes
Journal of microbiology and biotechnology, 24(7), 969-978 (2014-04-20)
The aprE2 gene with its prosequence from Bacillus subtilis CH3-5 was overexpressed in Escherichia coli BL21(DE3) by using plasmid pET26b(+). After IPTG induction, active and mature AprE2 was produced when cells were grown at 20°C, whereas inactive and insoluble enzyme
The hydrolysis of N-benzoyl-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide and its use as a substrate for the assay of cathepsin B.
Thrombin is an endolytic serine protease that selectively cleaves the Arg–Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.
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