Glutathione Peroxidase 1 Human ELISA

Research topic

Oxidative stress

Storage/Shipping

All kit components of this kit are stable at 2 to 8°C. Any unused reconstituted standard should be discarded or frozen at –70°C. Standard can be frozen and thawed one time only without loss of immunoreactivity.

Summary

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. Because Gpx1 appears to have a major role in the prevention of oxidative stress, it may also be an important antiatherogenic enzyme. In mice, Gpx1 deficiency results in abnormal vascular and cardiac function and structure. From a clinical perspective, there is a report suggesting that low erythrocyte Gpx1 activity identifies patients with coronary artery disease who are at the high risk for cardiovascular events and that measurement of Gpx1 activity provides additional information on risk and might be useful in identifying patients who would benefit from preventive antioxidant treatment.

Assay format

Sandwich ELISA, HRP-labelled antibody

Applications

Cell lysate, Plasma, Serum

Calibration range

0–100 ng/ml

Limit of detection

1.56 ng/ml

Intra-assay (Within-Run, n=7)

CV = 3.7 %

Inter-assay (Run-to-Run, n=8)

CV = 6.5 %

References to this product

• Takebe G, Yarimizu J, Saito Y, Hayashi T, Nakamura H, Yodoi J, Nagasawa S, Takahashi K. A comparative study on the hydroperoxide and thiol specificity of the glutathione peroxidase family and selenoprotein P. J Biol Chem. 2002 Oct 25;277 (43):41254-8
• De Haan JB, Crack PJ, Flentjar N, Iannello RC, Hertzog PJ, Kola I. An imbalance in antioxidant defense affects cellular function: the pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse. Redox Rep. 2003;8 (2):69-79
• Perry AC, Jones R, Niang LS, Jackson RM, Hall L. Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon. Biochem J. 1992 Aug 1;285 ( Pt 3):863-70
• Blankenberg S, Rupprecht HJ, Bickel C, Torzewski M, Hafner G, Tiret L, Smieja M, Cambien F, Meyer J, Lackner KJ. Glutathione peroxidase 1 activity and cardiovascular events in patients with coronary artery disease. N Engl J Med. 2003 Oct 23;349 (17):1605-13
• Avissar N, Eisenmann C, Breen JG, Horowitz S, Miller RK, Cohen HJ. Human placenta makes extracellular glutathione peroxidase and secretes it into maternal circulation. Am J Physiol. 1994 Jul;267 (1 Pt 1):E68-76
• Bao Y, Jemth P, Mannervik B, Williamson G. Reduction of thymine hydroperoxide by phospholipid hydroperoxide glutathione peroxidase and glutathione transferases. FEBS Lett. 1997 Jun 30;410 (2-3):210-2
• Chambers I, Frampton J, Goldfarb P, Affara N, McBain W, Harrison PR. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J. 1986 Jun;5 (6):1221-7