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19246-18-5

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19246-18-5 Usage

Uses

Cys-Gly has been used for derivatization by p-hydroxymercury benzoate (PHMB) for calibration of reversed phase chromatography coupled on-line and sequentially with a UV?visible diode array detector (RPLC-DAD).

Definition

ChEBI: A dipeptide consisting of glycine having an L-cysteinyl attached to its alpha-amino group. It is an intermediate metabolite in glutathione metabolism.

General Description

Cys-Gly, a dipeptide is a catabolic byproduct of glutathione.

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

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Loring,du Vigneaud

, p. 385,387 (1935)

-

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.

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.

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