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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.

19246-18-5

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19246-18-5 Usage

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.

Check Digit Verification of cas no

The CAS Registry Mumber 19246-18-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,9,2,4 and 6 respectively; the second part has 2 digits, 1 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 19246-18:
(7*1)+(6*9)+(5*2)+(4*4)+(3*6)+(2*1)+(1*8)=115
115 % 10 = 5
So 19246-18-5 is a valid CAS Registry Number.
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

19246-18-5SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name L-cysteinylglycine

1.2 Other means of identification

Product number -
Other names Cys-Gly-OH

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:19246-18-5 SDS

19246-18-5Related 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

19246-18-5Relevant articles and documents

OXYLIPIN-PEPTIDE CONJUGATED MEDIATORS THAT PROMOTE RESOLUTION OF INFECTION, ORGAN PROTECTION AND TISSUE REGENERATION

-

Sheet 8/34, (2016/05/02)

A family of bioactive compounds identified in self-resolving inflammatory exudates is disclosed. The compounds give UV chromophores characteristic of a conjugated triene double bond system coupled to an auxochrome allylic to the triene. Further elucidation of the compounds reveals that they have an oxylipin backbone conjugated to a peptide or amino acid moiety via an auxochrome. In some embodiments the auxochrome is sulfur. However, the auxochrome may be NH, CH2 or O. The compounds have potent bioactivity, in vitro, and, in vivo, including promoting resolution of infection, stimulating macrophage phagocytosis of bacteria; protecting tissues from neutrophil mediated damage, promoting tissue repair and regeneration and preventing or limiting second organ reflow/reperfusion damage.

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

Imaoka, Masashi,Yano, Shigekazu,Okumura, Masashi,Hibi, Takao,Wakayama, Mamoru

experimental part, p. 1936 - 1939 (2011/06/11)

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.

Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity

Castellano,Merlino, Antonello,Rossi, Mosè,La Cara, Francesco

experimental part, p. 464 - 474 (2011/11/30)

Gamma-glutamyltranspeptidases (γ-GTs) catalyze the transfer of the gamma-glutamyl moiety of glutathione and related gamma-glutamyl amides to water (hydrolysis) or to amino acids and peptides (transpeptidation) and play a key role in glutathione metabolism. Recently, γ-GTs have been considered attractive pharmaceutical targets for cancer and useful tools to produce γ-glutamyl compounds. To find out γ-GTs with special properties we have chosen microorganisms belonging to Geobacillus species which are source of several thermostable enzymes of potential interest for biotechnology. γ-GT from Geobacillus thermodenitrificans (GthGT) was cloned, expressed in Escherichia coli, purified to homogeneity and characterized. The enzyme, synthesized as a precursor homotetrameric protein of 61-kDa per subunit, undergoes an internal post-translational cleavage of the 61 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits. The kinetic characterization of the hydrolysis reaction using l-glutamic acid γ-(4-nitroanilide) as the substrate reveals that the active enzyme has Km 7.6 μM and Vmax 0.36 μmol min/mg. The optimum pH and temperature for the hydrolysis activity are 7.8 and 52 °C, respectively. GthGT hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress. Unlike other γ-GTs, the mutation of the highly conserved catalytic nucleophile, Thr353, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action. Furthermore, GthGT does not show any transpeptidase activity, suggesting that the enzyme is a specialized γ-glutamyl hydrolase. The GthGT homology-model structure reveals peculiar structural features, which should be responsible for the different functional properties of the enzyme and suggests the structural bases of protein thermostability.

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

Nakano, Yoshihiro,Okawa, Satoshi,Yamauchi, Takayoshi,Koizumi, Yukio,Sekiya, Jiro

, p. 369 - 376 (2008/02/10)

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.

Protease inhibitory polypeptides derived from urinary trypsin inhibitor and compositions thereof

-

, (2008/06/13)

This invention provides a novel polypeptide which comprises an amino acid sequence that constitutes a portion of urinary trypsin inhibitor (UTI) and which has no antigenicity against human and high activity to inhibit various proteases, as well as other novel polypeptides having excellent activities to inhibit various proteases obtained by mutation of the former novel polypeptide. This invention also provides novel enzyme inhibition processes, drug compositions and treating methods making use of the novel polypeptide, DNA fragments containing nucleotide sequences which encode the novel polypeptides, vectors containing the DNA fragments and transformants transformed with the DNA fragments or the vectors, as well as processes for the production of the novel polypeptides.

Characterization of novel isocyanate-derived metabolites of the formamide N-formylamphetamine with the combined use of electrospray mass spectrometry and stable isotope methodology

Borel,Abbott

, p. 891 - 899 (2007/10/03)

Bioactivation of the formamide N-formylamphetamine (NFA) to 1-methyl-2- phenylethyl isocyanate (MPIC) was investigated in rats by screening bile and urine for conjugates subsequent to the phase I event. NFA was administered to rats as a mixture of protio- and pentadeuteriophenyl analogues to gain insight into the carbamoylating activity of MPIC when traced by electrospray liquid chromatography/mass spectrometry (LC/MS). An LC/MS contour generated by recording the summed mass spectrum as a function of chromatographic retention time allowed four biliary metabolites to be identified from four sets of doublets, with the peak of each doublet offset by 5 amu and ca. 0.07 min. Tandem mass spectrometry experiments allowed these metabolites to be attributed structurally to the glutathione, cysteinylglycine, cysteine, and N-acetylcysteine conjugates of the isocyanate MPIC. These assignments were subsequently validated by comparison of the LC/MS properties of the metabolites to synthetic reference compounds. Only the carbamoylated N- acetylcysteine conjugate was detected in urine. The observed excretion in bile of all metabolites of the mercapturate pathway is novel for formamide metabolism. NFA can thus be added to the short list of compounds that are eliminated in this fashion. Factors envisioned as contributory to this metabolic profile in bile include hepatorenal, enterohepatic, and biliary- hepatic cycling, in addition to possible equilibrium exchange of the isocyanate from thiocarbamate conjugates to endogenous free thiols during the course of biliary transit.

Improved efficiency and selectivity in peptide synthesis: Use of triethylsilane as a carbocation scavenger in deprotection of t-butyl esters and t-butoxycarbonyl-protected sites

Mehta, Anita,Jaouhari, Rabih,Benson, Timothy J.,Douglas, Kenneth T.

, p. 5441 - 5444 (2007/10/02)

The use of triethylsilane as a carbocation scavenger in the presence of trifluoroacetic acid in dichloromethane leads to increased yields, decreased reaction times, simple work-up and improved selectivity for the deprotection of t-butyl ester and t-butoxycarbonyl sites in protected amino-acids and peptides in the presence of other acid-sensitive protecting groups such as the benzyloxycarbonyl, 9-fluorenylmethoxycarbonyl, O- and S-benzyl and t-butylthio groups.

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