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
[Clinical evaluation of prothrombin assay using chromogenic peptide substrates (author's transl)].
Y Akiyama et al.
Rinsho byori. The Japanese journal of clinical pathology, 28(11), 1131-1135 (1980-11-01)
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
Gnathostoma spinigerum is a causative agent of human gnathostomiasis and infects people residing in endemic areas as well as travelers. Cutaneous and visceral larval migrants cause clinical manifestations, resulting in severe morbidity and mortality. To survive in hosts, these parasites
The Factor VIII content of Factor IX concentrates was investigated by agarose gel electrophoresis which removed the interfering effects of stabilisers and proteolytic enzyme inhibitors. Factor VIII coagulant activity (FVIII C) as measured by clotting and amidolytic methods correlated well
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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