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2578-84-9

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2578-84-9 Usage

General Description

Z-Phe-ONP, also known as N-(3-(2-Furyl)acryloyl)-Phe-ONp, is a chemical compound often used in scientific and medical research. It is a type of synthetic substrate used to measure the activity of proteolytic enzymes, specifically chymotrypsin, an enzyme responsible for protein breakdown. Z-Phe-ONP is also used in enzyme specificity studies due to its change in color, which allows for accurate quantification. It is known for its sensitivity and specificity to the targeted enzymes. However, information on its toxicity or potential hazards is not widely available, indicating that uptake and biodegradability studies may still be needed.

Check Digit Verification of cas no

The CAS Registry Mumber 2578-84-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,5,7 and 8 respectively; the second part has 2 digits, 8 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 2578-84:
(6*2)+(5*5)+(4*7)+(3*8)+(2*8)+(1*4)=109
109 % 10 = 9
So 2578-84-9 is a valid CAS Registry Number.
InChI:InChI=1/C23H20N2O6/c26-22(31-20-13-11-19(12-14-20)25(28)29)21(15-17-7-3-1-4-8-17)24-23(27)30-16-18-9-5-2-6-10-18/h1-14,21H,15-16H2,(H,24,27)/t21-/m0/s1

2578-84-9SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 15, 2017

Revision Date: Aug 15, 2017

1.Identification

1.1 GHS Product identifier

Product name (4-nitrophenyl) 3-phenyl-2-(phenylmethoxycarbonylamino)propanoate

1.2 Other means of identification

Product number -
Other names L-4-nitrophenyl N-(benzyloxycarbonyl)phenylalanine

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:2578-84-9 SDS

2578-84-9Relevant articles and documents

Catalysis in peptide synthesis with active esters. I. Bifunctional catalysis in the aminolysis of benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester in dioxane.

Nakamizo

, p. 1071 - 1077 (1969)

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Synthesis and evaluation of peptidic irreversible inhibitors of tissue transglutaminase

Pardin, Christophe,Gillet, Steve M.F.G.,Keillor, Jeffrey W.

, p. 8379 - 8385 (2008/02/05)

Herein we report the synthesis and the evaluation of eight novel compounds as irreversible inhibitors of transglutaminase (TGase). These compounds are based on a minimal peptidic scaffold shown previously [Chem. Biol. 2005, 12, 469-475] to confer affinity for the TGase active site and bear electrophilic groups such as α,β-unsaturated amide, chloroacetamide or maleimide; their general structure being Cbz-Phe-spacer-electrophile. The affinity conferred by the Cbz-Phe scaffold was determined by comparison to N-propylacrylamide and the length of the spacer was also varied to evaluate its importance. The inhibitory efficiencies (kinact/KI) of these compounds vary up to 105 M-1 min-1, among the highest reported for derivatives based on this simple Cbz-Phe peptidic scaffold.

Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes

Yano, Yoshihiro,Shimada, Kenji,Okai, Jiro,Goto, Koichi,Matsumoto, Yoko,Ueoka, Ryuichi

, p. 1314 - 1318 (2007/10/03)

The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-α-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-α-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl- D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified α-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.

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