Home  >  Products  >  GSTO1, 140 D, Recombinant, Human (GSTTLp28, P28, glutathione S-transferase omega 1-1, glutathione transferase omega, glutathione transferase omega 1, glutathione-S-transferase like, Monomethyl Arsenous Reductase)

GSTO1, 140 D, Recombinant, Human (GSTTLp28, P28, glutathione S-transferase omega 1-1, glutathione transferase omega, glutathione transferase omega 1, glutathione-S-transferase like, Monomethyl Arsenous Reductase)

Cat no: G8135-21J


Supplier: United States Biological
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GSTO1 is a member of the theta class glutathione S-transferase-like (GSTTL) protein family. GSTO1 is expressed in a wide range of human tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities and also catalyzes the reduction of monomethylarsonate, an intermediate in the pathway of arsenic biotransformation. GSTO1 protects from oxidative stress, a risk factor for Alzheimer disease, vascular dementia and stroke. Several polymorphisms in the coding regions of the human GSTO1 have been identified. A polymorphism causing an alanine-to-aspartate (A140D) substitution in aa140 produces a variant with lowered enzyme activities in the arsenic biotransformation. Source: Recombinant corresponding to aa1-241 from human 140D mutant mature GSTO1, fused to 6x His-tag at N-terminal, expressed in E. coli. Applications: Suitable for use in Western Blot as a control. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: G8135-21J
Applications: Western Blot
Size: 10ug
Form: Supplied as a liquid in 25mM Tris-HCl, pH6.8, 50mM DTT, 1% SDS, 0.1% Bromophenol Blue, 2.5% glycerol.
Purity: Purified (SDS-PAGE)
References: 1. Withbread, A. K. et al., Methods in Enzymology 2005; 401: 78-99. 2. K

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