SOD Human His
Superoxide Dismutase Human Recombinant His Tag
Cat. No.
BT4753
Source
Escherichia Coli.
Synonyms
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Usage
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.
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Description
SOD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 189 amino acids with a 10 × His at N-terminus and having a molecular mass of 40.0kDa.
The SOD Human is purified by proprietary chromatographic techniques.
The SOD Human is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Human Cu/Zn Superoxide Dismutase (SOD1) is an enzyme that provides cellular protection against superoxide radicals. It catalyzes the conversion of superoxide anions to molecular oxygen and hydrogen peroxide. SOD1 is one of three SOD isozymes responsible for eliminating free superoxide radicals in the body. This enzyme plays a crucial role in protecting cells from damage caused by uncontrolled levels of superoxide. Mutations in the SOD1 gene are linked to a familial form of amyotrophic lateral sclerosis.
Description
Recombinant Human SOD, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 189 amino acids, includes a 10x His tag at the N-terminus, and has a molecular weight of 40.0 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile, white, lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 μm filtered solution in phosphate-buffered saline (PBS) at pH 7.4.
Solubility
To reconstitute the lyophilized SOD, it is recommended to dissolve it in sterile 18 MΩ-cm H₂O to a concentration of at least 100 μg/ml. This solution can then be further diluted in other aqueous solutions.
Stability
Lyophilized Human SOD remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, Human SOD should be stored at 4°C for 2-7 days. For future use, store it at -18°C. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% based on SDS-PAGE and HPLC analyses.
Biological Activity
The biological activity is confirmed to be comparable to the standard. Specific activity, measured using the Pyrogallic Acid method, is greater than 10,000 Units/mg.
Synonyms
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
Source
Escherichia Coli.
Amino Acid Sequence
MGHHHHHHHH HHSSGHIEGR HMTYARAAAR QARALEATKA VCVLKGDGPV QGIINFEQKE SNGPVKVWGS IKGLTEGLHG FHVHEFGDNT AGCTSAGPHF NPLSRKHGGP KDEERHVGDL GNVTADKDGV ADVSIEDSVI SLSGDHCIIG RTLVVHEKAD DLGKGGNEES TKTGNAGSRL ACGVIGIAQ
Product Science Overview
Introduction
Superoxide dismutase (SOD) is a critical enzyme in the defense against oxidative stress in biological systems. It catalyzes the dismutation of the superoxide radical (O2•−) into oxygen and hydrogen peroxide, thereby protecting cells from damage caused by reactive oxygen species (ROS). The human recombinant form of SOD with a His tag is a genetically engineered version of this enzyme, designed for enhanced purification and stability.
Types of Superoxide Dismutase
There are three main types of SOD in humans:
- SOD1 (Cu/Zn-SOD): Found in the cytoplasm, it binds copper and zinc ions and is responsible for neutralizing superoxide radicals in the cytosol .
- SOD2 (Mn-SOD): Located in the mitochondria, it binds manganese ions and plays a crucial role in protecting mitochondrial components from oxidative damage .
- SOD3 (EC-SOD): An extracellular enzyme that also binds copper and zinc ions, it is involved in protecting tissues from extracellular superoxide radicals .
Human Recombinant SOD with His Tag
The recombinant form of SOD is produced using bacterial expression systems, such as Escherichia coli. The His tag, a sequence of histidine residues, is added to the N- or C-terminus of the protein to facilitate purification through affinity chromatography. This tag allows for efficient isolation of the enzyme from bacterial lysates, ensuring high purity and yield.
Applications
Recombinant SOD with a His tag is widely used in research and therapeutic applications:
- Oxidative Stress Studies: It is used to study the effects of oxidative stress and the role of SOD in mitigating ROS-induced damage.
- Therapeutic Potential: SOD has potential therapeutic applications in conditions characterized by oxidative stress, such as neurodegenerative diseases, cardiovascular diseases, and inflammatory conditions.
- Biochemical Research: The His-tagged recombinant SOD is used in various biochemical assays to understand its structure, function, and interaction with other molecules.
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