Glutathione Peroxidase, Human, Western Blot Control

Highly reactive and potentially dangerous reactive oxygen species (ROS) are normally produced within the cells, primarily from the mitochondrial respiratory chain where in excess electrons are donated to molecular oxygen (o2) to generate peroxide anion (O2-). Superoxide anion is reduced by the superoxide dismutase (SOD) to hydrogen peroxide (H2O2) and hydrogen peroxide is reduced to water (H2O) by catalase, located primarily in the peroxisomes, and by glutathione peroxidase (GPx), located in the mitochondria and cytosol. Hydrogen peroxide, in the presence of transitions metals, can be converted to the highly toxic hydroxyl radical (OH.) and all three of the ROS (O2-, H2O2, and OH.) can damage macromolecules (proteins, DNA etc). The GPxs are commonly considered the most important for ROS defense since they have broader substrate specificities and stronger affinity for H2O2 than catalases.\nTwo of the main types of glutathione peroxidases (GPxs) that have been characterized in cells are the classical GPx (cGPx) and the phospholipid hydroperoxide GPx (PHGPx). cGPx is multimeric (commonly tetrameric) and soluble, whereas PHGPx is monomeric and often membrane-associated. In addition, whereas cGPx has specificity for glutathione as a reducing substrate, PHGPx re-reduction may be coupled to alternative systems such as the thioredoxin pathway . Thus, PHGPx is often considered the principal cellular enzyme capable of repairing membrane lipid peroxidation, the highly damaging process that has been linked to pathological conditions such as ischemic injury, atherosclerosis, and carcinogenesis. Human GPX1 (Glutathione peroxidase 1 or GSHPx-1 or Cellular glutathione peroxidase, 201-aa, chromosome 3p21.3) contains Selenium in the form of selenocysteine. GPX is one of only a few proteins known in higher vertebrates to contain selenocysteine. This unusual amino acid occurs at the active site of GPX and is coded by the nonsense (stop) scodon TGA. Neonatal deficiency of the selenoenzyme glutathione peroxidase, with hematologic consequences, may result from 'selenium imbalance' during pregnancy.\n\nSource:\nPurified Human GPX from red cells (erythrocytes)\n\nApplications:\nSuitable for use in Western Blot as a control. Load 10ul/lane for good visibility with antibody Cat # G8127-01. Other applications not tested.\n\nNote: SDS may crystallize in cold conditions. It should redissolve by warming before taking it from the stock. It should be heated once prior to loading on gels. If the product has been stored for several weeks, then it may be preferable to add 5ul of fresh 2X sample buffer per 10ul of the solution prior to heating and loading on gels. This preparation is not biologically active. It is not suitable for ELISA or other applications where native protein is required. This preparation is intended for qualitative purpose and not to serve as standard of known concentration.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months 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

G8127-01A

Size

50ul

Applications

WB

Form

Supplied as a liquid in SDS-PAGE sample buffer (reduced).

References

Maddipati KR et al (1987) JBC 262, 17398-17403; Takahasi K et al (1990) J. Biochem. 108, 145-148; Esworhty RS et al (1991) Arch Biochem. Biophys. 286, 330-336; Yoshimuar S et al (1994) Gene 145, 293-297