SOD Human, 15N
Greater than 95.0% as determined by SDS-PAGE Analysis.
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 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.
Product Specs
Human Cu/Zn Superoxide Dismutase (SOD) is an enzyme that catalyzes the breakdown of superoxide radicals into hydrogen peroxide and molecular oxygen. This process is crucial for protecting cells from the harmful effects of superoxide radicals. SOD contains copper and zinc ions and is one of three isozymes responsible for eliminating free superoxide radicals in the body. The protein encoded by the SOD1 gene neutralizes superoxide molecules, preventing cellular damage caused by their uncontrolled levels.
Recombinant Human Superoxide Dismutase, 15N is a protein produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 153 amino acids, with a molecular weight of 15.8 kDa.
The product is lyophilized from a 0.2 μm filtered solution at a concentration of 1 mg/ml in PBS containing 0.1 mM CuCl2 and 0.2 mM ZnCl2.
The purity of the product is determined to be greater than 95.0% by SDS-PAGE analysis.
ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGD NTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSV ISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ.
Product Science Overview
Superoxide dismutase (SOD) is a crucial enzyme that plays a significant role in protecting cells from oxidative stress by catalyzing the dismutation of superoxide radicals into oxygen and hydrogen peroxide. The human recombinant form of this enzyme, labeled with nitrogen-15 (^15N), is particularly valuable for scientific research due to its enhanced stability and traceability in various experimental settings.
Superoxide dismutase exists in several isoforms, with the most common being the copper-zinc (CuZn-SOD), manganese (Mn-SOD), and iron (Fe-SOD) variants. The human recombinant SOD, often produced in Escherichia coli, retains the essential structural and functional characteristics of the native enzyme. The ^15N labeling allows for detailed nuclear magnetic resonance (NMR) studies, providing insights into the enzyme’s structure, dynamics, and interactions at the atomic level .
The primary function of SOD is to catalyze the conversion of superoxide radicals (O_2^•−) into molecular oxygen (O_2) and hydrogen peroxide (H_2O_2). This reaction is vital for mitigating the harmful effects of reactive oxygen species (ROS) in biological systems. The enzyme’s active site typically contains metal ions, such as copper and zinc, which facilitate the redox reactions necessary for dismutation .
The recombinant form of SOD, especially when labeled with ^15N, is extensively used in various research fields, including biochemistry, molecular biology, and medicine. Some key applications include:
- Structural Studies: ^15N-labeled SOD is instrumental in NMR spectroscopy, allowing researchers to study the enzyme’s structure and dynamics in detail.
- Oxidative Stress Research: SOD is a critical tool for investigating the mechanisms of oxidative stress and its role in diseases such as cancer, neurodegenerative disorders, and cardiovascular diseases.
- Therapeutic Potential: Due to its antioxidative properties, SOD has potential therapeutic applications in treating conditions associated with oxidative damage, such as inflammation, ischemia-reperfusion injury, and aging .
The production of recombinant SOD involves cloning the human SOD gene into an expression vector, which is then introduced into a suitable host, such as E. coli. The bacteria are cultured under conditions that promote the expression of the recombinant protein. The ^15N labeling is achieved by growing the bacteria in a medium containing ^15N-labeled compounds. The protein is then purified using techniques such as affinity chromatography and characterized to ensure its activity and stability .
