Recombinant Human Epididymal secretory glutathione peroxidase (GPX5) is produced in E. coli and features an N-terminal 6xHis-GST tag that makes purification straightforward. This full-length Isoform 2 protein contains amino acids 1-100 and shows a purity level greater than 85% as determined by SDS-PAGE. This product is intended for research use only and is not suitable for diagnostic or therapeutic applications.
Epididymal secretory glutathione peroxidase (GPX5) is an antioxidant enzyme that appears to play a crucial role in protecting cells from oxidative stress by reducing lipid hydroperoxides and hydrogen peroxide. It belongs to the glutathione peroxidase family, which seems integral to cellular defense mechanisms against reactive oxygen species. GPX5 may be particularly relevant in reproductive biology, where it's involved in maintaining the integrity of sperm cells.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Biochemical Characterization and Enzyme Kinetics Studies
This recombinant GPX5 protein can be used to investigate the fundamental biochemical properties of human epididymal secretory glutathione peroxidase. This includes substrate specificity, optimal pH and temperature conditions, and cofactor requirements. The N-terminal His-GST tag makes purification and immobilization easier for detailed kinetic analyses. Researchers might compare the enzymatic properties of this truncated form (1-100aa) with full-length GPX5 to understand structure-function relationships. The high purity level (>85%) makes it suitable for quantitative biochemical assays and mechanistic studies.
2. Antibody Development and Validation
The recombinant GPX5 protein serves as an excellent immunogen and standard for developing specific antibodies against human GPX5. The His-GST tag allows easy purification and quantification for consistent antibody production protocols. Researchers can use this protein to validate antibody specificity, determine binding affinities, and establish detection limits in various immunoassays. The defined protein sequence and purity appear ideal for generating both polyclonal and monoclonal antibodies for subsequent research applications.
3. Protein-Protein Interaction Studies
The dual His-GST tag system makes this recombinant GPX5 particularly well-suited for pull-down assays to identify potential binding partners or interacting proteins in epididymal tissue extracts or other relevant biological samples. The GST tag allows for glutathione-based affinity purification while the His tag provides an alternative purification strategy and detection method. Researchers can investigate how GPX5 may interact with other antioxidant enzymes, structural proteins, or regulatory molecules in the male reproductive system.
4. Comparative Structural and Functional Analysis
This truncated GPX5 construct (1-100aa) can be used in comparative studies to understand the functional domains and structural requirements of glutathione peroxidase family members. Researchers might analyze how this N-terminal region contributes to overall protein stability, folding, and potential catalytic activity compared to other GPX isoforms. The recombinant protein enables detailed biophysical characterization including circular dichroism spectroscopy, dynamic light scattering, and thermal stability analyses to understand the structural properties of this specific GPX5 region.
