19246-18-5

Basic information

• Product Name: CYS-GLY
• Synonyms: L-CYSTEINYL GLYCINE;L-CYSTEINYLGLYCINE MONOHYDRATE;CYS-GLY;H-CYS-GLY-OH;cysteinylglycine;glycine,n-cysteinyl;n-l-cysteinyl-glycin;2-(2-amino-3-sulfanyl-propanoyl)aminoacetic acid
• CAS NO: 19246-18-5
• Molecular Formula: C₅H₁₀N₂O₃S
• Molecular Weight: 178.21
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 19246-18-5.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 459oC at 760 mmHg
• Flash Point: 231.4oC
• Appearance: /
• Density: 1.373g/cm3
• Vapor Pressure: 1.06E-09mmHg at 25°C
• Refractive Index: 1.557
• Storage Temp.: −20°C
• Solubility: DMSO (Slightly), Methanol (Slightly), Water (Slightly)
• PKA: 3.02±0.10(Predicted)
• Stability: Air Sensitive
• CAS DataBase Reference: CYS-GLY(CAS DataBase Reference)
• NIST Chemistry Reference: CYS-GLY(19246-18-5)
• EPA Substance Registry System: CYS-GLY(19246-18-5)

Safety Data

• Hazard Codes: Xn
• Statements: 22-36
• Safety Statements: 26
• WGK Germany: 3
• RTECS: MB9285800
• Hazardous Substances Data: 19246-18-5(Hazardous Substances Data)

Usage

Description

CYS-GLY, also known as Cys-Glycine, is a dipeptide consisting of glycine with an L-cysteinyl attached to its alpha-amino group. It is an intermediate metabolite in glutathione metabolism and serves as a catabolic byproduct of glutathione.

Uses

Used in Chromatography:
CYS-GLY is used as a derivatization agent for p-hydroxymercury benzoate (PHMB) in the calibration of reversed phase chromatography. This application is particularly useful for coupling on-line and sequentially with a UV-visible diode array detector (RPLC-DAD), enhancing the accuracy and efficiency of the chromatographic process.
Used in Pharmaceutical Industry:
CYS-GLY, being a part of glutathione metabolism, has potential applications in the pharmaceutical industry. It can be utilized in the development of drugs targeting glutathione-related pathways, which may have implications for various therapeutic areas, including antioxidant defense, detoxification, and immune system regulation.
Used in Research and Development:
CYS-GLY can be employed as a research tool for studying the role of glutathione in cellular processes and its involvement in various diseases. This can lead to a better understanding of glutathione metabolism and the development of novel therapeutic strategies targeting this pathway.
Used in Analytical Chemistry:
CYS-GLY can be used as a reference compound or standard in analytical chemistry for the development and validation of new methods and techniques for the analysis of peptides and other related compounds. This can contribute to the advancement of analytical methodologies and the improvement of existing ones.

Biochem/physiol Actions

Cys-Gly is a precursor for glutathione biosynthesis in the neurons. It favors reactive oxygen species generation in the presence of transition metal ions. A normal level of cys-gly is essential for normal cellular function.

InChI:InChI=1/C5H10N2O3S/c6-3(2-11)5(10)7-1-4(8)9/h3,11H,1-2,6H2,(H,7,10)(H,8,9)/t3-/m0/s1

Upstream product

• 70-18-8 GLUTATHIONE 
• 74527-65-4 N-((R)-3-formyl-2,2-dimethyl-thiazolidine-4-carbonyl)-glycine 
• 2601-46-9 Z-L-Cys(Bzl)-Gly-OBzl 
• 166036-87-9 N-tert-butoxycarbonyl-S-(3,4-dimethylbenzyl)-L-cysteinylglycine 
• 7732-18-5 water 
• 2790-86-5 (Z-L-Cys-GlyOH)2 
• 7664-41-7 ammonia 
• 556-50-3 glycylglycine 
• 149227-97-4 N-((R)-3-formyl-2,2-dimethyl-thiazolidine-4-carbonyl)-glycine-methyl ester 

Downstream Products

• 4909-66-4 N-[N-(N-benzyloxycarbonyl-Ξ-γ-glutamyl)-L-cysteinyl]-glycine 
• 7729-20-6 L-cystinyl-bis-glycine 
• 127041-56-9 (6E,8E,10E)-(S)-5-Hydroxy-11-(1-methoxy-4-pentyl-cyclohexyl)-undeca-6,8,10-trienoic acid methyl ester 
• 91944-21-7 7Z,9E,11E,14Z-LTD₄ methyl ester 
• 91944-21-7 (7E,9E,11Z,14Z)-6-[2-Amino-2-(carboxymethyl-carbamoyl)-ethylsulfanyl]-5-hydroxy-icosa-7,9,11,14-tetraenoic acid methyl ester 
• 20933-67-9 R(-)-2-thioxothiazolidine-4-carboxylic acid 
• 7669-84-3 S-benzyl-L-cysteinylglycine 
• 79695-13-9 LTD5 
• 77165-74-3 Leukotrien D3 
• 73836-78-9 7Z,9E,11E,14Z-LTD₄ 
• 52-90-4 L-Cysteine 

Related news

Binding of Hg2+ by Cys, CYS-GLY (cas 19246-18-5) and reduced glutathione: Study by differential pulse voltammetry on rotating Au-disk electrode, electrospray ionization mass-spectrometry and isothermal titration calorimetry08/03/2019

The study of Hg2+ binding with short-chain thiols as cysteine (Cys), dipeptide Cys-Gly and reduced glutathione (GSH) was performed by a recently proposed voltammetric method, using the rotating Au-disk electrode. For every thiol a similar complexation pattern was obtained. The highly stable Hg(t...detailed

Relevant articles and documents

-

-

Molecular cloning and characterization of γ-Glutamyltranspeptidase from pseudomonas nitroreducens IFO12694

y-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydro-lytic activity than transfer activity, as compared with other y-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard y-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a y-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.

Purification and properties of soluble and bound γ- glutamyltransferases from radish cotyledon

Soluble and cell wall bound γ-glutamyltransferases (GGTs) were purified from radish (Raphanus sativus L.) cotyledons. Soluble GGTs (GGT I and II) had the same Mr of 63,000, and were composed of a heavy subunit (Mr, 42,000) and a light one (Mr, 21,000). The properties of GGT I and II were similar. Bound GGTs (GGT A and B) were purified to homogeneity from the pellet after the extraction of soluble GGTs. GGT A and B were monomeric proteins with an Mr of 61,000. The properties of GGT A and B were similar. Thus, bound GGTs were distinguished from soluble GGTs. The optimal pHs of soluble and bound GGTs were about 7.5. Both soluble and bound GGTs utilized glutathione, γ-L-glutamyl-p-nitroanilide, oxidized glutathione and the conjugate of glutathione with monobromobimane as substrates, and were inhibited by acivicin, but soluble GGTs were also distinguished from bound GGTs with regard to these properties.