GPX7 Human

The GPX7 gene is located on chromosome 1 at the 1p32.3 region . The gene contains three distinct introns and produces four different mRNA transcripts through alternative splicing . The protein itself is a non-selenocysteine-containing enzyme, which differentiates it from other members of the glutathione peroxidase family .

The recombinant human GPX7 protein is typically produced in E. coli or HEK293 cells. It is a single, non-glycosylated polypeptide chain containing 193 amino acids, with a molecular mass of approximately 21.8 kDa . The recombinant protein is often fused with tags such as His-tag or Fc region of human IgG1 to facilitate purification and detection .

GPX7 exhibits glutathione peroxidase activity, which involves the reduction of hydrogen peroxide and organic hydroperoxides using glutathione as a substrate . This activity is crucial for cellular defense against oxidative stress, which can cause damage to proteins, lipids, and DNA. GPX7 is also involved in the metabolism of arachidonic acid and glutathione .

GPX7 is expressed in various tissues, including the extracellular space and endoplasmic reticulum . It plays a significant role in cellular responses to oxidative stress and detoxification of cellular oxidants . The enzyme has been implicated in several physiological and pathological processes, including bone turnover and response to oxidative stress .

Mutations or dysregulation of the GPX7 gene have been associated with certain diseases, such as amnestic disorder and Keshan disease . Additionally, GPX7 has been studied for its potential role in cancer, particularly in alleviating oxidative stress in breast cancer cells .

Recombinant human GPX7 is widely used in research to study its function and role in various biological processes. It is also utilized in drug development and therapeutic applications aimed at mitigating oxidative stress-related damage .