Share this post on:

Product: Propyphenazone

Recombinant Human Glutathione Peroxidase 5 Protein Summary

Description
Glutathione Peroxidase 5 (Human) GST-Tagged Recombinant Protein

Source: Wheat Germ (in vitro)

Amino Acid Sequence: MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYVGKHILFVNVATYCGLTAQYPGMSVQGEDLYLVSSFLRKGM

Protein/Peptide Type
Recombinant Protein
Gene
GPX5

Applications/Dilutions

Application Notes
Useful in Western Blot and ELISA. This protein has not been tested for any functionality. This product may contain endotoxins and is not suitable for use with live cells.

Packaging, Storage & Formulations

Storage
Store at -80C. Avoid freeze-thaw cycles.
Buffer
50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0 in the elution buffer.

Notes

This product is produced by and distributed for Abnova, a company based in Taiwan.

Alternate Names for Recombinant Human Glutathione Peroxidase 5 Protein

  • EC 1.11.1
  • EC 1.11.1.9
  • EGLP
  • epididymal androgen-related protein
  • epididymal secretory glutathione peroxidase
  • Epididymis-specific glutathione peroxidase-like protein
  • glutathione peroxidase 5 (epididymal androgen-related protein)
  • Glutathione peroxidase 5
  • GPx-5
  • GSHPx-5

Background

Glutathione peroxidase (GPX)/glutathione reductase is part of the hydrogen peroxide scavenging system found within the epididymis in the mammalian male reproductive tract. GPX5 expression is epididymis-specific and the transcript is unique from other GPXs because it contains a deletion resulting in an mRNA that does not contain a selenocysteine (UGA) codon (an unusual amino acid present in other GPXs). This deletion also renders the mRNA incapable of encoding an active GPX isoenzyme. For this reason, GPX5 is selenium-independent and has very little activity towards hydrogen peroxide or organic hydroperoxides. GPX5, which is bound to the acrosome of sperm, may act to protect sperm from premature acrosome reaction in the epididymis. [provided by RefSeq]

PMID: 23349051

Share this post on:

Author: Potassium channel