SODA E.Coli

Superoxide Dismutase E.Coli Recombinant
Cat. No.
BT5187
Source
Escherichia Coli.
Synonyms
Superoxide dismutase [Mn], MnSOD, soda, b3908, JW3879.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

SODA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-206 a.a.) and having a molecular mass of 25.2kDa.
SODA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Superoxide dismutase Mn (soda), a member of the iron/manganese superoxide dismutase family, plays a crucial role in cellular defense against oxidative stress. It catalyzes the conversion of superoxide radicals (O2-) into less harmful molecules like oxygen (O2) and hydrogen peroxide (H2O2). Subsequently, these byproducts are further detoxified by enzymes like catalase and glutathione peroxidase, resulting in the production of water (H2O) and oxygen (O2).
Description
Produced in E. coli, SODA is a single, non-glycosylated polypeptide chain composed of 226 amino acids (specifically, amino acids 1 to 206). It has a molecular weight of 25.2 kDa. For purification purposes, a 20 amino acid His-tag is fused to the N-terminus of SODA, and proprietary chromatographic techniques are employed.
Physical Appearance
The product is a clear and sterile solution without any color.
Formulation
SODA E.coli solution is provided at a concentration of 1mg/ml. The solution is buffered with 20mM Tris-HCl at a pH of 8.0 and supplemented with 1mM DTT, 10% glycerol, and 0.1M NaCl.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it should be kept frozen at -20°C. The addition of a carrier protein like HSA or BSA (0.1%) is advised for long-term storage. It is important to avoid repeated cycles of freezing and thawing.
Purity
The purity of the product is determined using SDS-PAGE analysis and is found to be greater than 95%.
Biological Activity
The specific activity of the enzyme is measured as its ability to inhibit the reduction of cytochrome c in a coupled system using xanthine and xanthine oxidase. With a reaction volume of 1.5 ml at pH 7.8 and a temperature of 25°C, the specific activity is greater than 350 units/mg. One unit is defined as the amount of enzyme required to inhibit the reduction rate of cytochrome c by 50%.
Synonyms
Superoxide dismutase [Mn], MnSOD, soda, b3908, JW3879.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA NLPVEELITK LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA AASRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS
GFPIMGLDVW EHAYYLKFQN RRPDYIKEFW NVVNWDEAAA RFAAKK.

Product Science Overview

Types of Superoxide Dismutase

There are three main types of superoxide dismutase based on their metal co-factors:

  1. Cu/Zn SOD: Found in the cytoplasm.
  2. Mn SOD: Located in the mitochondria.
  3. Fe SOD: Present in prokaryotes and some plants.
Recombinant Superoxide Dismutase

Recombinant superoxide dismutase is produced using genetic engineering techniques where the SOD gene is inserted into a host organism, such as Escherichia coli (E. coli), to produce the enzyme in large quantities. This method ensures a consistent and high-purity product suitable for research and therapeutic applications.

Production in E. coli

E. coli is a preferred host for recombinant protein production due to its rapid growth, well-understood genetics, and ability to express high levels of protein. The process involves:

  1. Gene Cloning: The SOD gene is cloned into a plasmid vector.
  2. Transformation: The plasmid is introduced into E. coli cells.
  3. Expression: E. coli cells are cultured under conditions that induce the expression of the SOD gene.
  4. Purification: The recombinant SOD is purified using chromatographic techniques to achieve high purity.
Characteristics of Recombinant SOD

Recombinant SOD produced in E. coli typically forms a homodimer consisting of two identical subunits. Each subunit contains 154 amino acids and has a molecular mass of approximately 31.6 kDa . The enzyme is highly active and stable, making it suitable for various applications.

Applications

Recombinant SOD has several applications, including:

  • Research: Studying oxidative stress and related cellular processes.
  • Therapeutics: Potential treatments for diseases caused by oxidative damage, such as neurodegenerative diseases and inflammatory conditions.
  • Cosmetics: Used in skincare products for its antioxidant properties.
Storage and Stability

Recombinant SOD is typically lyophilized for storage and can be reconstituted in sterile water or buffer. It is stable for several months when stored at -20°C to -70°C and should be protected from repeated freeze-thaw cycles to maintain its activity .

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