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Z-Leu-Gly-Ome, also known as carbobenzoxy-L-leucyl-glycine methyl ester, is a dipeptide with a molecular formula of C16H24N2O5 and a molecular weight of 320.37 g/mol. It is a chemical compound often utilized in biochemical research, particularly known for its role as a substrate in enzyme-catalyzed reactions, specifically involving proteolytic enzymes such as elastase and cathepsin G. Z-Leu-Gly-Ome is generally available in a stable, solid form and should be stored in a cool, dry location to maintain its integrity. However, like many chemicals, it poses potential risks if not handled correctly, and it's important to use protective equipment when handling Z-Leu-Gly-Ome.

5084-98-0

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5084-98-0 Usage

Uses

Used in Biochemical Research:
Z-Leu-Gly-Ome is used as a substrate for enzyme-catalyzed reactions, particularly in the study of proteolytic enzymes such as elastase and cathepsin G. This application aids in understanding the mechanisms and functions of these enzymes, which are crucial in various biological processes.
Used in Pharmaceutical Development:
Z-Leu-Gly-Ome is used as a potential candidate for the development of new drugs targeting proteolytic enzymes. By studying its interactions with these enzymes, researchers can gain insights into the design of more effective therapeutic agents for treating diseases associated with abnormal proteolytic activity.
Used in Diagnostic Applications:
Z-Leu-Gly-Ome can be used as a diagnostic tool to assess the activity of proteolytic enzymes in biological samples. This can help in the early detection and monitoring of diseases where these enzymes play a significant role, such as certain types of cancer and inflammatory conditions.
Used in Educational Purposes:
Z-Leu-Gly-Ome is used as a teaching aid in academic institutions to demonstrate the principles of enzyme kinetics and the role of substrates in enzyme-catalyzed reactions. This helps students understand the fundamental concepts of biochemistry and the importance of proteolytic enzymes in various biological processes.

Check Digit Verification of cas no

The CAS Registry Mumber 5084-98-0 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,0,8 and 4 respectively; the second part has 2 digits, 9 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 5084-98:
(6*5)+(5*0)+(4*8)+(3*4)+(2*9)+(1*8)=100
100 % 10 = 0
So 5084-98-0 is a valid CAS Registry Number.
InChI:InChI=1/C17H24N2O5/c1-12(2)9-14(16(21)18-10-15(20)23-3)19-17(22)24-11-13-7-5-4-6-8-13/h4-8,12,14H,9-11H2,1-3H3,(H,18,21)(H,19,22)

5084-98-0SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name Z-LEU-GLY-OME

1.2 Other means of identification

Product number -
Other names methyl N-benzyloxycarbonyl-L-leucylglicynate

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:5084-98-0 SDS

5084-98-0Relevant articles and documents

Recyclable hypervalent iodine(III) reagent iodosodilactone as an efficient coupling reagent for direct esterification, amidation, and peptide coupling

Tian, Jun,Gao, Wen-Chao,Zhou, Dong-Mei,Zhang, Chi

supporting information; experimental part, p. 3020 - 3023 (2012/08/07)

A hypervalent iodine(III) reagent plays a novel role as an efficient coupling reagent to promote the direct condensation between carboxylic acids and alcohols or amines to provide esters, macrocyclic lactones, amides, as well as peptides without racemization. The regeneration of iodosodilactone (1) can also be readily achieved. The intermediate acyloxyphosphonium ion C from the activation of a carboxylic acid is thought to be involved in the present esterification reaction.

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH

Vishwanatha,Narendra,Chattopadhyay, Basab,Mukherjee, Monika,Sureshbabu, Vommina V.

experimental part, p. 2689 - 2702 (2012/06/01)

Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.

SYNTHESIS OF FRAGMENTS OF THE VP1 PROTEIN OF TYPE A22 FOOT-AND-MOUTH DISEASE VIRUS. SYNTHESIS OF FRAGMENTS 134-139, 134-145, 140-145, 150-155, AND 150-159

Khalikov, Sh. Kh.,Alieva, S. V.,Ashurov, S. G.

, p. 202 - 212 (2007/10/02)

Fragments of peptides of the amino acid sequences (134-145) and (150-159) of the VP1 protein of the type A22 foot-and-mouth disease (FMD)virus have been synthesized by the classical methods of peptide chemistry.Oligopeptides were obt

KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS

Hoogwater, D. A.,Peereboom, M.

, p. 5325 - 5332 (2007/10/02)

The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.

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