Skip to Content
Merck
All Photos(1)

Key Documents

View All Documentation

G0903

Sigma-Aldrich

γ-Glu-Cys

≥80% (HPLC), suitable for ligand binding assays

Synonym(s):

γ-L-Glutamyl-L-cysteine, des-Gly-glutathione reduced form

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

Empirical Formula (Hill Notation):
C8H14N2O5S
CAS Number:
636-58-8
Molecular Weight:
250.27
MDL number:
MFCD00237863
UNSPSC Code:
12352209
PubChem Substance ID:
24895030
NACRES:
NA.26

product name

γ-Glu-Cys, ≥80% (HPLC)

Quality Level

200

Assay

≥80% (HPLC)

form

powder

composition

Peptide content, ≥60% elemental analysis

technique(s)

ligand binding assay: suitable

color

white to off-white

storage temp.

−20°C

SMILES string

N[C@@H](CCC(=O)N[C@@H](CS)C(O)=O)C(O)=O

InChI

1S/C8H14N2O5S/c9-4(7(12)13)1-2-6(11)10-5(3-16)8(14)15/h4-5,16H,1-3,9H2,(H,10,11)(H,12,13)(H,14,15)/t4-,5-/m0/s1

InChI key

RITKHVBHSGLULN-WHFBIAKZSA-N

Looking for similar products? Visit Product Comparison Guide

Amino Acid Sequence

Glu-Cys

Application

γ-Glu-Cys is used to study the active sites and kinetics of glutathione synthetase(s). It has also been used for the extraction and quantification of low molecular weight thiols from Arabidopsis tissues.

Biochem/physiol Actions

γ-L-Glutamyl-L-cysteine (γ-Glu-Cys) is a substrate used for the biosynthesis of L-glutathione by glutathione synthetase(s). γ-Glu-Cys is generated by the cleavage of the Cys-Gly peptide bond of glutathione. It is also essential for the formation of phytochelatins, which are cysteine-rich thiol-reactive peptides.

Physical form

Lyophilized from 0.1% TFA.

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H315,H319,H335

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

T Hara et al.
Protein engineering, 8(7), 711-716 (1995-07-01)
Lys18, Arg86, Asn283, Ser286, Thr288 and Glu292 of glutathione synthetase from Escherichia coli B are presumed to be highly concerned with the substrate, gamma-L-glutamyl-L-cysteine (gamma-Glu-Cys), binding by X-ray crystallography and affinity labeling studies. Using site-directed mutagenesis, we investigated functional roles
Helmut Schweikl et al.
Dental materials : official publication of the Academy of Dental Materials, 37(1), 175-190 (2020-12-12)
The release of inflammatory cytokines from antigen-stimulated cells of the immune system is inhibited by resin monomers such as 2-hydroxyethyl methacrylate (HEMA). Although the formation of oxidative stress in cells exposed to HEMA is firmly established, the mechanism behind the
Method for determination of free and total glutathione and gamma-glutamylcysteine concentrations in human leukocytes and plasma.
J Mårtensson
Journal of chromatography, 420(1), 152-157 (1987-09-04)
H Yamaguchi et al.
Journal of molecular biology, 229(4), 1083-1100 (1993-02-20)
Glutathione synthetase (gamma-L-glutamyl-L-cysteine: glycine ligase (ADP-forming) EC 6.3.2.3: GSHase) catalyzes the synthesis of glutathione from gamma-L-glutamyl-L-cysteine and Gly in the presence of ATP. The enzyme from Escherichia coli is a tetramer with four identical subunits of 316 amino acid residues.
Runa Njålsson et al.
Human genetics, 116(5), 384-389 (2005-02-18)
Glutathione synthetase (GS) deficiency is a rare autosomal recessive disorder. The clinical phenotype varies widely, and nearly 30 different mutations in the GSS gene have been identified. In the present study, genotype, enzyme activity, metabolite levels and clinical phenotype were
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service