추천 제품
product name
Z-Phe-Leu,
분석
≥98% (TLC)
형태
powder
기술
ligand binding assay: suitable
색상
white
저장 온도
−20°C
SMILES string
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
생화학적/생리학적 작용
N-CBZ-Phe-Leu (Z-phe-Ieu) (CBZ-phenylalanylleucine) is an N-terminal protected Cbz-dipeptide substrate used to differentiate, characterize and kinetically analyze various carboxypeptidase(s).
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
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
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
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
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
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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