B6760
N-Benzoyl-L-tyrosine p-nitroanilide
≥98.0% (TLC)
别名:
Benzoyl-L-tyrosine p-nitroanilide
产品名称
N-Benzoyl-L-tyrosine p-nitroanilide,
方案
≥98.0% (TLC)
表单
powder
颜色
white
mp
235-237 °C
储存温度
−20°C
SMILES字符串
Oc1ccc(CC(NC(=O)c2ccccc2)C(=O)Nc3ccc(cc3)[N+]([O-])=O)cc1
InChI
1S/C22H19N3O5/c26-19-12-6-15(7-13-19)14-20(24-21(27)16-4-2-1-3-5-16)22(28)23-17-8-10-18(11-9-17)25(29)30/h1-13,20,26H,14H2,(H,23,28)(H,24,27)
InChI key
CJERUMAUMMIPRF-UHFFFAOYSA-N
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相关类别
应用
N-Benzoyl-L-tyrosine p-nitroanilide (BTPNA) is used as a substrate to identify, differentiate and characterize serine carboxypeptidase(s) and various proteases.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
J Suh et al.
Bioorganic & medicinal chemistry letters, 8(11), 1331-1336 (1999-01-01)
Both activity and stability of alpha-Chymotrypsin (ChT) are substantially enhanced in the microdomains of laurylated or benzylated derivatives of poly(ethylenimine). EPR data revealed that the enhancement in activity of ChT is due to increase in the polarity of the microenvironment
A Gervaix et al.
Journal of immunology (Baltimore, Md. : 1950), 147(6), 1912-1919 (1991-09-15)
The effects of carbobenzyloxy-leucine-tyrosine-chloromethylketone (zLYCK), an inhibitor of chymotrypsin, were investigated on the activation pathways of the human neutrophil respiratory burst. At 10 microM zLYCK, a parallel inhibition was observed of superoxide production stimulated with the chemo-attractant FMLP and of
Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes.
von Elert E, Agrawal MK, et al.
Comp. Biochem. Physiol., B: Comp. Biochem., 137, 287-296 (2004)
G Colebatch et al.
Insect biochemistry and molecular biology, 31(4-5), 415-423 (2001-02-27)
Protease activities in the secreted saliva, salivary glands and midgut of the green mirid, Creontiades dilutus, were investigated. The saliva and salivary glands had more protease activity than the midgut, but no differences in protease activity levels were detected between
Mai Makino et al.
FEBS open bio, 9(7), 1337-1343 (2019-06-08)
Yeast carboxypeptidase Y (CPY) is a serine protease with broad substrate specificity. Structurally, CPY belongs to the α/β hydrolase fold family and contains characteristic large helices, termed the V-shape helix, above the active site cavity. Four intramolecular disulfide bonds are
商品
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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