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Hexylglutathione Sale

(Synonyms: S-Hexylglutathione, NSC 131114) 目录号 : GC46154

An mtMGST1 inhibitor

Hexylglutathione Chemical Structure

Cas No.:24425-56-7

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100mg
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Sample solution is provided at 25 µL, 10mM.

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产品描述

Hexylglutathione is a mitochondrial membrane-bound microsomal glutathione S-transferase 1 (mtMGST1) inhibitor (IC50 = 0.48 mM).1 It also inhibits the dopachrome tautomerase activity of macrophage migration inhibitory factor (MIF; IC50 = 3.3 mM).2 It has been used as an affinity chromatography ligand to purify glutathione S-transferase (GST) from sheep liver homogenate.3

|1. Ulziikhishig, E., Lee, K.K., Hossain, Q.S., et al. Inhibition of mitochondrial membrane bound-glutathione transferase by mitochondrial permeability transition inhibitors including cyclosporin A. Life Sci. 86(19-20), 726-732 (2010).|2. Swope, M.D., Sun, H.W., Klockow, B., et al. Macrophage migration inhibitory factor interactions with glutathione and S-hexylglutathione. J. Biol. Chem. 273(24), 14877-14884 (1998).|3. Reddy, C.C., Burgess, Z.Z., Gong, Z.Z., et al. Purification and characterization of the individual glutathione S-transferases from sheep liver. Arch. Biochem. Biophys. 224(1), 87-101 (1983).

Chemical Properties

Cas No. 24425-56-7 SDF
别名 S-Hexylglutathione, NSC 131114
Canonical SMILES CCCCCCSC[C@@H](C(NCC(O)=O)=O)NC(CC[C@H](N)C(O)=O)=O
分子式 C16H29N3O6S 分子量 391.5
溶解度 DMSO: slightly soluble,DMSO:PBS (pH 7.2) (1:2): 0.3mg/mL 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 2.5543 mL 12.7714 mL 25.5428 mL
5 mM 0.5109 mL 2.5543 mL 5.1086 mL
10 mM 0.2554 mL 1.2771 mL 2.5543 mL
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Research Update

Characterization of glutathione S-transferases from day-old chick livers

Biochemistry 1990 Jan 23;29(3):744-50.PMID:2337594DOI:10.1021/bi00455a022.

Glutathione S-transferases (GSTs, EC 2.5.1.18) were isolated from the liver cytosolic fraction of 1 day old Leghorn chicks by S-hexylglutathione and glutathione affinity columns arranged in tandem. After sample loading, the affinity columns were detached from each other and developed separately. Four groups of GSTs (CL 1, 2, 3, and 4) were eluted from the Hexylglutathione column, and an additional group of GSTs (CL 2 and 5) was eluted from the glutathione affinity column. CL 2, CL 3, and CL 5 were further purified to homogeneity by chromatofocusing, and the substrate specificities of each group were determined. Fractions from the chromatofocusing column were analyzed by native IEF electrophoresis. Protein bands were electroblotted onto PVDF membrane for N-terminal sequence analysis or extracted from IEF gel and rerun on SDS-PAGE to determine the subunit composition of each GST dimer. CL 2, CL 3, and CL 5 can form homodimers, whereas CL 1 and CL 4 exist only as CL 1-2 and CL 3-4 heterodimers. CL 2 and CL 5 have N-terminal amino acid sequences homologous to rat liver Yb and Ya GSTs, respectively. CL 1 has a unique N-terminal sequence that is not homologous to any known GSTs.