Copper Chaperone for Superoxide Dismutase Human Recombinant
CCS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294amino acids (1-274a.a.) and having a molecular wieght of 31.2kDa. The CCS is fused to a 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Superoxide Dismutase Human Recombinant
Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a non-glycosylated homodimeric polypeptide chain containing 2 x 153 amino acids and having a total molecular mass of 31.6kDa.
Superoxide Dismutase Human Recombinant His Tag
Superoxide Dismutase, 15N Human Recombinant
Recombinant Human Superoxide Dismutase, 15N produced in E.Coli is a single non-glycosylated polypeptide chain containing 153 amino acids and having a total molecular mass of 15.8kDa.
Superoxide Dismutase 1 Human Recombinant
Superoxide Dismutase-2 Human Recombinant
Superoxide Dismutase-2 Mouse Recombinant
Superoxide Dismutase E.Coli Recombinant
Superoxide dismutase (SOD) is a crucial enzyme that catalyzes the dismutation of the superoxide radical (O₂⁻) into oxygen (O₂) and hydrogen peroxide (H₂O₂). This enzyme plays a vital role in protecting cells from oxidative damage caused by reactive oxygen species (ROS). SODs are classified based on their metal cofactor and protein fold into three major families:
Primary Biological Functions: SODs play a critical role in protecting cells from oxidative damage by converting superoxide radicals into hydrogen peroxide and oxygen. This process is vital for cellular defense against oxidative stress .
Role in Immune Responses and Pathogen Recognition: SODs are involved in modulating immune responses by regulating the levels of ROS, which are crucial for pathogen recognition and elimination. They help in maintaining the redox balance during immune responses .
Mechanisms with Other Molecules and Cells: SODs interact with various molecules and cells to neutralize superoxide radicals. The enzyme alternates between reduced and oxidized states to facilitate the conversion of superoxide radicals into hydrogen peroxide and oxygen .
Binding Partners and Downstream Signaling Cascades: SODs bind to metal cofactors (copper, zinc, manganese, iron, or nickel) to catalyze the dismutation reaction. This process is crucial for initiating downstream signaling cascades that protect cells from oxidative damage .
Transcriptional Regulation: The expression of SOD genes is regulated by various transcription factors that respond to oxidative stress. For example, the transcription factor Nrf2 plays a significant role in upregulating SOD expression in response to increased ROS levels .
Post-Translational Modifications: SODs undergo various post-translational modifications, such as phosphorylation and acetylation, which can affect their activity and stability .
Biomedical Research: SODs are extensively studied for their role in protecting cells from oxidative damage and their potential therapeutic applications in diseases associated with oxidative stress .
Diagnostic Tools: SOD activity is used as a biomarker for oxidative stress in various diseases, including neurodegenerative disorders and cardiovascular diseases .
Therapeutic Strategies: SOD mimetics and gene therapy approaches are being developed to enhance SOD activity in conditions where oxidative stress plays a significant role .
Development to Aging and Disease: SODs play a crucial role throughout the life cycle, from development to aging. They help in maintaining cellular homeostasis and protecting against age-related diseases by mitigating oxidative damage. SODs are also involved in the defense against intracellular pathogens, ensuring the survival of cells under oxidative stress .