Welcome to LookChem.com Sign In|Join Free

CAS

  • or
Z-TYR-LEU-NH2 is a synthetic peptide composed of the amino acids tyrosine (TYR) and leucine (LEU), with an amide group (NH2) at the end. It serves as a model compound in research and drug development, aiding in the study of peptide interactions and behavior within biological systems. Z-TYR-LEU-NH2's structure and properties are instrumental in exploring the structure-activity relationships of peptides and in the design of new peptide-based therapeutics.

17331-91-8

Post Buying Request

17331-91-8 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

17331-91-8 Usage

Uses

Used in Pharmaceutical Research:
Z-TYR-LEU-NH2 is used as a model compound for studying the interactions of peptides with biological systems, which is crucial for understanding their behavior and potential therapeutic effects.
Used in Drug Development:
Z-TYR-LEU-NH2 is utilized as a template in the development of peptide-based drugs, providing insights into the structural requirements for biological activity.
Used in Neurotransmitter Modulation Research:
Z-TYR-LEU-NH2 is used as a research tool to explore its potential role in modulating neurotransmitter activity, which could have implications for the treatment of neurological disorders.
Used in Therapeutic Agent Development for Neurological Disorders:
Z-TYR-LEU-NH2 is considered as a potential therapeutic agent for conditions such as neurological disorders, given its effects on neurotransmitter activity.
Used in Therapeutic Agent Development for Chronic Pain:
Z-TYR-LEU-NH2 is also being studied for its potential as a therapeutic agent for chronic pain, suggesting that it may have analgesic properties.
Used in Structure-Activity Relationship Studies:
Z-TYR-LEU-NH2 is used in research to determine the relationship between the chemical structure of peptides and their biological activities, which is vital for the design of effective peptide-based drugs.

Check Digit Verification of cas no

The CAS Registry Mumber 17331-91-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,7,3,3 and 1 respectively; the second part has 2 digits, 9 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 17331-91:
(7*1)+(6*7)+(5*3)+(4*3)+(3*1)+(2*9)+(1*1)=98
98 % 10 = 8
So 17331-91-8 is a valid CAS Registry Number.

17331-91-8SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name Z-TYR-LEU-NH2

1.2 Other means of identification

Product number -
Other names -

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:17331-91-8 SDS

17331-91-8Downstream Products

17331-91-8Relevant articles and documents

Studies on Enzymatic Peptide Synthesis in Biphasic Aqueous-Organic Systems with Product Extraction

Kuhl, Peter,Schaaf, Regina,Jakubke, Hans-Dieter

, p. 1279 - 1288 (1987)

The dipeptide derivatives Z-Tyr-Leu-NH2 and Mca-Tyr-Leu-NH2 were synthesized by α-chymotrypsin-catalyzed coupling reactions in solvent systems consisting of buffer and ethyl acetate.In comparison to a pure aqueous medium, in which only insignificant synth

ENZYME PEPTIDE SYNTHESIS BY AN ITERATIVE PROCEDURE IN A NUCLEOPHILE POOL

Petkov, D. D.,Stoineva, I. B.

, p. 3751 - 3754 (1984)

An effective method for enzyme solubility-controlled synthesis of peptides, consisting in an iterative addition of equivalent amounts of acyl and amine components to a solution(nucleophile pool) containing the enzyme and a large excess of the amine component, is described.

Enzymatic C-terminal amidation of amino acids and peptides

Nuijens, Timo,Piva, Elena,Kruijtzer, John A.W.,Rijkers, Dirk T.S.,Liskamp, Rob M.J.,Quaedflieg, Peter J.L.M.

experimental part, p. 3777 - 3779 (2012/09/22)

Herein, we describe two versatile and high yielding enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic amidation reactions proceeded much faster without side reactions and gave near to quantitative yields of products.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 17331-91-8