SOD Human
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
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.
Product Specs
Recombinant Human Cu/Zn Superoxide Dismutase, expressed in E. coli, is a non-glycosylated homodimeric protein. Each of the two identical polypeptide chains consists of 153 amino acids, resulting in a total molecular weight of 31.6kDa.
The purity of the product is greater than 95.0%, as determined by two methods: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis and (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
The biological activity of the product, measured using the Pyrogallic Acid method, is greater than 3,000 Units/mg.
ATKAVCVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEF GDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH CIIGRTLVVH EKADDLGKGG NEESTKTGNA GSRLACGVIG IAQ.
Product Science Overview
There are three main types of SOD in mammals:
- Cu/Zn-SOD (SOD1): Found in the cytosol, mitochondrial intermembrane space, and nucleus.
- Mn-SOD (SOD2): Located in the mitochondrial matrix.
- Extracellular SOD (SOD3): Present in the extracellular space .
These enzymes play a pivotal role in maintaining cellular homeostasis by preventing oxidative damage to DNA, proteins, and lipids .
Recombinant human superoxide dismutase (rhSOD) is produced using genetic engineering techniques. It is typically expressed in microbial systems such as Escherichia coli or Bacillus subtilis. The recombinant enzyme retains the same functional properties as the naturally occurring enzyme, making it a valuable tool for research and therapeutic applications .
The production of rhSOD involves cloning the human SOD gene into a suitable expression vector, which is then introduced into a host organism. The host cells are cultured under optimized conditions to maximize the expression of rhSOD. The enzyme is subsequently purified using chromatographic techniques to ensure high purity and activity .
- Medical Applications: rhSOD has been investigated for its potential therapeutic benefits in conditions associated with oxidative stress, such as neurodegenerative diseases, cancer, and inflammatory disorders. It has shown promise in reducing oxidative damage and improving clinical outcomes in various experimental models .
- Cosmetic Applications: Due to its antioxidant properties, rhSOD is also used in cosmetic formulations to protect the skin from oxidative damage and reduce signs of aging .
- Food Industry: rhSOD is utilized in the food industry to enhance the shelf life of products by preventing oxidative spoilage .
Despite its potential, the application of rhSOD faces several challenges, including issues related to membrane permeability and the stability of the enzyme in vivo. Ongoing research aims to address these challenges by developing more effective delivery systems and enhancing the stability of rhSOD .
In conclusion, recombinant human superoxide dismutase is a powerful antioxidant enzyme with diverse applications in medicine, cosmetics, and the food industry. Continued research and development are expected to further expand its utility and effectiveness in combating oxidative stress-related conditions.
