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.
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 30(8), 1085-1096 (2000-08-10)
Fel d 1, an important allergen from domestic cats, is a significant cause of asthma. In addition to directly promoting IgE synthesis, other biological activities of allergens may contribute to either allergic sensitization or the magnitude of allergic effector responses.
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
In this study, sulfated polysaccharide-rich extracts were isolated from 22 tropical seaweeds (4 red, 11 brown, and 7 green) found in northeastern Brazil, and evaluated for the role of anticoagulant agents. Fifteen of the extracts showed anticoagulant activity, including all
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
Substrates for determination of trypsin, thrombin and thrombin-like enzymes.
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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