SOD1 Recombinant Proteins 

SOD1 (Superoxide Dismutase 1) recombinant proteins are engineered forms of the enzyme that plays a crucial role in cellular defense against oxidative stress. SOD1 catalyzes the dismutation of superoxide radicals into hydrogen peroxide and oxygen, protecting cells from reactive oxygen species (ROS)-induced damage.

Content

• Structure and Function:
  • SOD1 is a metalloenzyme with a dimeric structure, binding copper and zinc ions for catalytic activity.
  • Mutations in the SOD1 gene are linked to familial ALS, making SOD1 a key protein for studying neurodegeneration.
• Expression Systems:
  • Bacterial Systems (e.g., E. coli): Cost-effective production of non-glycosylated SOD1 variants.
  • Mammalian Systems: Suitable for producing SOD1 with post-translational modifications.
  • Insect Cells: Balances yield and structural fidelity.
• Quality Control:
  • Purity: Confirmed by SDS-PAGE and size-exclusion chromatography.
  • Activity: Assessed using colorimetric or fluorometric assays for ROS scavenging.
  • Structural Validation: Verified using X-ray crystallography or circular dichroism spectroscopy.

Applications

• Oxidative Stress Studies:
  • Exploring cellular mechanisms of ROS detoxification and redox homeostasis.
  • Evaluating the effects of oxidative stress in various cell and tissue models.
• Structural and Biophysical Analysis:
  • Elucidating the structure-function relationships of SOD1 and its mutants.
  • Studying metal ion binding and its role in enzymatic activity.
• Drug Discovery:
  • High-throughput screening of SOD1 modulators for ALS and other oxidative stress-related disorders.
  • Testing antioxidant therapies targeting ROS detoxification pathways.

SOD1 recombinant proteins are pivotal in advancing our understanding of oxidative stress, protein misfolding disorders, and therapeutic development for diseases such as ALS. Their versatility and biochemical relevance make them invaluable tools in both basic and applied research.