产品名称
N-Benzoyl-L-tyrosine p-nitroanilide,
SMILES string
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
assay
≥98.0% (TLC)
form
powder
color
white
mp
235-237 °C
storage temp.
−20°C
Quality Level
Application
N-Benzoyl-L-tyrosine p-nitroanilide (BTPNA) is used as a substrate to identify, differentiate and characterize serine carboxypeptidase(s) and various proteases.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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
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)
Bernardo Ramírez-Zavala et al.
International journal of food microbiology, 91(3), 245-252 (2004-02-27)
We purified a carboxypeptidase (CPY) from the yeast of Kluyveromyces marxianus. This enzyme was purified 170 times from a soluble extract of 100000 x g. Purification consisted in a fractionated precipitation with ammonium sulfate and two chromatographic steps consisting of
K S LIU et al.
The Analyst, 115(8), 1143-1144 (1990-08-01)
In assaying chymotrypsin inhibition by the soybean Bowman-Birk inhibitor, two sequences of mixing the reactants were tried: adding the substrate last (s-last test) or adding the enzyme last (e-last test). The inhibition values obtained from the s-last test were either
Caterina Temporini et al.
Journal of separation science, 30(17), 3069-3076 (2007-10-11)
The preparation and optimization of a new monolithic chymotrypsin bioreactor for online protein digestion is described. Silica monolithic supports have been activated with epoxide functionalities following an optimized in situ procedure and used for covalent immobilization of chymotrypsin in one-step
商品
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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