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H6886

Sigma-Aldrich

S-Hexylglutathione

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

Synonyme(s) :

S-Hexyl-L-glutathione reduced

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About This Item

Formule empirique (notation de Hill):
C16H29N3O6S
Numéro CAS:
24425-56-7
Poids moléculaire :
391.48
Numéro Beilstein :
5629635
Numéro MDL:
MFCD00056735
Code UNSPSC :
12352209
ID de substance PubChem :
329815236
Nomenclature NACRES :
NA.26

product name

S-Hexylglutathione,

Pureté

>98% (TLC)

Forme

powder

Technique(s)

ligand binding assay: suitable

Pf

200-202 °C

Température de stockage

2-8°C

Chaîne SMILES 

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

Clé InChI

HXJDWCWJDCOHDG-RYUDHWBXSA-N

Catégories apparentées

Amino Acid Sequence

S-Hexyl-Glu-Cys-Gly

Application

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

Actions biochimiques/physiologiques

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).

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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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
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
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
Y Hathout et al.
Chemical research in toxicology, 9(6), 1044-1049 (1996-09-01)
Interaction of chlorambucil and the glutathione-depleted human placenta pi class glutathione S-transferase (pi GST) results in the formation of a complex between the drug and the protein at physiological pH. This complex is not formed in the presence of glutathione
Liqing Chen et al.
Acta crystallographica. Section D, Biological crystallography, 59(Pt 12), 2211-2217 (2003-12-04)
Glutathione S-transferases (GSTs) are a major family of detoxification enzymes which possess a wide range of substrate specificities. Most organisms possess many GSTs belonging to multiple classes. Interest in GSTs in insects is focused on their role in insecticide resistance;
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