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H6886

Sigma-Aldrich

S-Hexylglutathione

>98% (TLC), suitable for ligand binding assays

Synonym(s):

S-Hexyl-L-glutathione reduced

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About This Item

Empirical Formula (Hill Notation):
C16H29N3O6S
CAS Number:
Molecular Weight:
391.48
Beilstein:
5629635
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26

Product Name

S-Hexylglutathione,

Assay

>98% (TLC)

Quality Level

form

powder

technique(s)

ligand binding assay: suitable

mp

200-202 °C

storage temp.

2-8°C

SMILES string

CCCCCCSC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(=O)NCC(O)=O

InChI

1S/C16H29N3O6S/c1-2-3-4-5-8-26-10-12(15(23)18-9-14(21)22)19-13(20)7-6-11(17)16(24)25/h11-12H,2-10,17H2,1H3,(H,18,23)(H,19,20)(H,21,22)(H,24,25)/t11-,12-/m0/s1

InChI key

HXJDWCWJDCOHDG-RYUDHWBXSA-N

Amino Acid Sequence

S-Hexyl-Glu-Cys-Gly

Application

Ligand useful for affinity chromatography of glutathione-S-transferase and glutathione peroxidase.

Biochem/physiol Actions

S-Hexylglutathione may be used as an affinity chromatography ligand of glutathione-S-transferase and glutathione peroxidase. S-Hexylglutathione is also used as an inhibitor to study the specificity and kinetics of enzymes such as mitochondrial membrane-bound glutathione transferase(s) (mtMGST1).

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

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M Bäck et al.
British journal of pharmacology, 133(7), 1134-1144 (2001-08-07)
Contractions of guinea-pig tracheal preparations to cysteinyl-leukotrienes (LTC(4), LTD(4) and LTE(4)) were characterized in organ baths, and cysteinyl-leukotriene metabolism was studied using radiolabelled agonists and RP-HPLC separation. In the presence of S-hexyl GSH (100 microM) the metabolism of [(3)H]-LTC(4) into
Emilee E Colón-Lorenzo et al.
Frontiers in pharmacology, 11, 246-246 (2020-04-08)
Plasmodium falciparum parasites are increasingly drug-resistant, requiring the search for novel antimalarials with distinct modes of action. Enzymes in the glutathione pathway, including glutathione S-transferase (GST), show promise as novel antimalarial targets. This study aims to better understand the biological
Natalya Kurochkina et al.
Journal of theoretical biology, 283(1), 92-102 (2011-05-31)
Helix-helix parallel interfaces can be characterized by certain combinations of amino acids, which repeatedly occur at core positions a and d (leucine zipper nomenclature) in homologous and nonhomologous proteins and influence interhelical angles. Applied for the prediction of interhelical angles
J M Stevens et al.
Biochemistry, 37(44), 15534-15541 (1998-11-04)
Solvent-induced equilibrium unfolding of a homodimeric class sigma glutathione transferase (GSTS1-1, EC 2.5.1.18) was characterized by tryptophan fluorescence, anisotropy, enzyme activity, 8-anilino-1-naphthalenesulfonate (ANS) binding, and circular dichroism. Urea induces a triphasic unfolding transition with evidence for two well-populated thermodynamically stable
Rosa M F Cardoso et al.
Proteins, 51(1), 137-146 (2003-02-22)
The 26-kDa glutathione S-transferase from Schistosoma japonicum (Sj26GST), a helminth worm that causes schistosomiasis, catalyzes the conjugation of glutathione with toxic secondary products of membrane lipid peroxidation. Crystal structures of Sj26GST in complex with glutathione sulfonate (Sj26GSTSLF), S-hexyl glutathione (Sj26GSTHEX)

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