推荐产品
产品名称
N-Benzoyl-L-tyrosine p-nitroanilide,
方案
≥98.0% (TLC)
质量水平
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)
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
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
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
Proteases in egg, miracidium and adult of Fasciola gigantica. Characterization of serine and cysteine proteases from adult.
Mohamed SA, Fahmy AS, et al.
Comp. Biochem. Physiol., B: Comp. Biochem., 142, 192-200 (2005)
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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