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Merck
CN

C1141

Sigma-Aldrich

Z-Phe-Leu

≥98% (TLC), suitable for ligand binding assays

别名:

N-CBZ-Phe-Leu

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About This Item

经验公式(希尔记法):
C23H28N2O5
CAS号:
分子量:
412.48
MDL编号:
UNSPSC代码:
12352209
PubChem化学物质编号:
NACRES:
NA.26

product name

Z-Phe-Leu,

检测方案

≥98% (TLC)

质量水平

形式

powder

技术

ligand binding assay: suitable

颜色

white

储存温度

−20°C

SMILES字符串

CC(C)CC(NC(=O)C(Cc1ccccc1)NC(=O)OCc2ccccc2)C(O)=O

InChI

1S/C23H28N2O5/c1-16(2)13-20(22(27)28)24-21(26)19(14-17-9-5-3-6-10-17)25-23(29)30-15-18-11-7-4-8-12-18/h3-12,16,19-20H,13-15H2,1-2H3,(H,24,26)(H,25,29)(H,27,28)

InChI key

IBOXOGVHBFUSFH-UHFFFAOYSA-N

Amino Acid Sequence

Z-Phe-Leu

生化/生理作用

N-CBZ-Phe-Leu(Z-phe-Ieu)(CBZ-苯丙氨酰亮氨酸)是一种N端保护的Cbz-二肽底物,可用于对多种羧肽酶进行区分、表征和动力学分析。

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

新产品

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R Raksakulthai et al.
Journal of agricultural and food chemistry, 49(10), 5019-5030 (2001-10-16)
The hepatopancreas of squid (Illex illecebrosus) extract contains a wide range of carboxypeptidase (CP) activities based on hydrolysis of N-CBZ-dipeptide substrates. SDS-PAGE zymograms with N-CBZ-Phe-Leu substrate revealed three activity zones (CP-I, 23 kDa; CP-II, 29 kDa; CP-III, 42 kDa). CP-I
H Ostrowska
Platelets, 8(5), 355-360 (2006-06-24)
Human platelets were investigated for activity of the acidic carboxypeptidases: cathepsin A, lysosomal carboxypeptidase B and prolyl-carboxypeptidase. It was found that the main acidic carboxypeptidase in human platelets had cathepsin A activity. No activity of lysosomal carboxypeptidase B and prolyl-carboxypeptidase
Long-Liu Lin et al.
Journal of biotechnology, 128(2), 322-334 (2006-11-30)
The gene encoding a Deinococcus radiodurans R1 bifunctional aminoacylase/carboxypeptidase (DR_ACY/CP) was amplified by polymerase chain reaction and cloned into pQE-30 to generate pQE-DRAC. The cloned gene consists of an open reading frame of 1197 bp encoding a protein with a
Joji Mima et al.
European journal of biochemistry, 269(13), 3220-3225 (2002-06-27)
Cys341 of carboxypeptidase Y, which constitutes one side of the solvent-accessible surface of the S1 binding pocket, was replaced with Gly, Ser, Asp, Val, Phe or His by site-directed mutagenesis. Kinetic analysis, using Cbz-dipeptide substrates, revealed that polar amino acids
Li Li et al.
Journal of industrial microbiology & biotechnology, 35(1), 41-47 (2007-10-19)
Effects of the enzymes in Actinomucor elegans extract and the enzyme Alcalase 2.4L on debittering the soybean protein hydrolysates were investigated. When the protein was treated only with the latter, a strong bitterness formed; but it decreased if the protein

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