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C1141

Sigma-Aldrich

Z-Phe-Leu

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

Sinónimos:

N-CBZ-Phe-Leu

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About This Item

Fórmula empírica (notación de Hill):
C23H28N2O5
Número de CAS:
4313-73-9
Peso molecular:
412.48
MDL number:
MFCD00038301
UNSPSC Code:
12352209
PubChem Substance ID:
24892360
NACRES:
NA.26

Nombre del producto

Z-Phe-Leu,

assay

≥98% (TLC)

Quality Level

200

form

powder

technique(s)

ligand binding assay: suitable

color

white

storage temp.

−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

Categorías relacionadas

Amino Acid Sequence

Z-Phe-Leu

Biochem/physiol Actions

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
BCCC5696
BCBV7740
BCBK6334V
BCBQ2760V
1417282V

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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
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
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
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
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

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