Recombinant Human GPX5 Protein, N-His

Reference: YHB29401
Product nameRecombinant Human GPX5 Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight24.29 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeMet28-Lys221
Aliases /SynonymsGSHPx-5, GPX5, Epididymal secretory glutathione peroxidase, EGLP, GPx-5, Glutathione peroxidase 5, Epididymis-specific glutathione peroxidase-like protein
ReferenceYHB29401
NoteFor research use only.

Description of Recombinant Human GPX5 Protein, N-His

Introduction
Recombinant Human GPX5 Protein, also known as Glutathione Peroxidase 5, is a member of the glutathione peroxidase family of antioxidant enzymes. This protein is encoded by the GPX5 gene and is found in various tissues such as the epididymis, prostate, and seminal vesicles. GPX5 is primarily involved in protecting cells from oxidative stress by catalyzing the reduction of hydrogen peroxide and organic hydroperoxides. In this article, we will discuss the structure, activity, and applications of Recombinant Human GPX5 Protein.

Structure
The Recombinant Human GPX5 Protein is a homotetramer, meaning it is composed of four identical subunits. Each subunit contains a selenocysteine residue at the active site, which is essential for the catalytic activity of the protein. The molecular weight of the protein is approximately 22 kDa and it has a pI of 5.5. The crystal structure of GPX5 has been determined, revealing a characteristic fold of the glutathione peroxidase family with a central helix surrounded by four beta strands.

Activity
The primary function of GPX5 is to protect cells from oxidative damage. This is achieved through its ability to reduce hydrogen peroxide and organic hydroperoxides using glutathione as a cofactor. GPX5 is also able to reduce lipid hydroperoxides, which are produced as a result of oxidative stress. This activity is crucial for maintaining the integrity of sperm cells, as they are highly susceptible to oxidative damage due to their high content of polyunsaturated fatty acids.

In addition to its antioxidant activity, GPX5 has been shown to have a role in sperm maturation. It has been suggested that GPX5 may be involved in the regulation of sperm capacitation, a process that prepares sperm for fertilization. This is supported by studies showing that GPX5 levels increase during sperm maturation and that GPX5-deficient mice have impaired fertility.

Applications
Recombinant Human GPX5 Protein has various applications in both research and clinical settings. One of the main applications is in the study of male fertility. As GPX5 plays a crucial role in sperm maturation and function, its levels and activity can be used as biomarkers for male infertility. In addition, studies have shown that GPX5 may be a potential target for male contraceptive development.

Another potential application of Recombinant Human GPX5 Protein is in the treatment of oxidative stress-related disorders. As GPX5 is involved in protecting cells from oxidative damage, it has been suggested that supplementing with this protein may help alleviate oxidative stress in conditions such as cardiovascular disease, neurodegenerative diseases, and male infertility.

Recombinant Human GPX5 Protein can also be used in the development of diagnostic assays for oxidative stress. As GPX5 is a key player in the antioxidant defense system, its levels and activity can be used to assess the extent of oxidative stress in various diseases and conditions.

Conclusion
In summary, Recombinant Human GPX5 Protein is a vital member of the glutathione peroxidase family with important roles in protecting cells from oxidative damage and regulating sperm maturation. Its structure, activity, and applications make it a valuable tool in research and potential therapeutic target for various disorders. Further studies on this protein may provide insights into its potential use in the diagnosis and treatment of oxidative stress-related diseases.

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