Glutathione Peroxidase 4, SelCys73Cys, Recombinant, Human (Phospholipid Hydroperoxide Glutathione Peroxidase, Mitochondrial, PHGPx, GPx-4, GSHPx-4, GPX4)

Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/ mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract. Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation. Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine. All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site.\n\nSource:\nRecombinant corresponding to aa25-197 (Cysteine is substituted for Sec73), human from Glutathione Peroxidase 4, expressed in E.coli.\n\nMolecular Weight:\n~19kD\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. 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.

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SPECIFICATIONS

Catalog Number

G8127-14R

Size

500ug

Form

Supplied as a lyophilized from 20mM HEPES, pH 7.4. Reconstitute with sterile dH2O PBS.

Purity

~95% (SDS-PAGE)

References

1. Takebe, G. et al. (2002) J. Biol. Chem. 277, 41254-41258. 2. Avissar, N. et al. (1994) Am. J. Physiol. 267, E68-76. 3. Bao, Y. et al. (1997) FEBS Lett. 410, 210-212. 4. Chambers, I. et al. (1986) EMBO J. 5, 1221-1227. 5. Perry, A. et al. (1992) Biochem. J. 285, 863-870.