Recombinant Proteins

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CEA
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SOD Human His

Superoxide Dismutase Human Recombinant His Tag

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.
Shipped with Ice Packs
Cat. No.
BT4753
Source
Escherichia Coli.
Appearance
Sterile, white, lyophilized (freeze-dried) powder.

SOD Human, 15N

Superoxide Dismutase, 15N Human Recombinant

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.

Shipped with Ice Packs
Cat. No.
BT4823
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

SOD1 Human

Superoxide Dismutase 1 Human Recombinant

Recombinant Human Cu/Zn Superoxide Dismutase, expressed in E.Coli, is a non-glycosylated polypeptide chain consisting of a single monomer. It comprises 154 amino acids and exhibits a molecular weight of 15.9 kDa. The purification of SOD1 is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4898
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered.

SOD2 Human

Superoxide Dismutase-2 Human Recombinant

This product consists of a single, non-glycosylated polypeptide chain of the human SOD2 protein. It is produced in E. coli and contains 219 amino acids (25-222 a.a.), with a molecular weight of 24.4 kDa. For purification purposes, a 20 amino acid His-Tag is fused to the N-terminus. The protein is purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT4991
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CCS Human

Copper Chaperone for Superoxide Dismutase Human Recombinant

Recombinant human CCS, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 294 amino acids (1-274a.a.) with a molecular weight of 31.2 kDa. The CCS protein is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4571
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

SOD Human

Superoxide Dismutase Human Recombinant

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.

Shipped with Ice Packs
Cat. No.
BT4673
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

SOD2 Mouse

Superoxide Dismutase-2 Mouse Recombinant

This product is a recombinant SOD2 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain with a molecular weight of 24.6 kDa. The protein consists of 221 amino acids (residues 25-222) and has a 23 amino acid His-tag at the N-terminus for purification. It is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5090
Source
Escherichia Coli.
Appearance
Clear, sterile solution.

SODA E.Coli

Superoxide Dismutase E.Coli Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT5187
Source
Escherichia Coli.
Appearance
The product is a clear and sterile solution without any color.
Definition and Classification

Superoxide dismutase (SOD) is a crucial enzyme that catalyzes the dismutation of the superoxide radical (O₂⁻) into oxygen (O₂) and hydrogen peroxide (H₂O₂). This enzyme plays a vital role in protecting cells from oxidative damage caused by reactive oxygen species (ROS). SODs are classified based on their metal cofactor and protein fold into three major families:

  • Cu/Zn SOD: Contains copper and zinc, commonly found in the cytosol of eukaryotic cells.
  • Mn SOD: Contains manganese, primarily located in the mitochondria.
  • Fe SOD: Contains iron, found in prokaryotes.
  • Ni SOD: Contains nickel, also found in prokaryotes .
Biological Properties

Key Biological Properties: SODs are metalloenzymes that detoxify superoxide radicals, converting them into less harmful molecules. They are essential for maintaining cellular redox balance and preventing oxidative stress .

Expression Patterns and Tissue Distribution:

  • SOD1 (Cu/Zn SOD): Predominantly found in the cytosol and nucleus of cells.
  • SOD2 (Mn SOD): Located in the mitochondria.
  • SOD3 (Cu/Zn SOD): Found in the extracellular matrix .
Biological Functions

Primary Biological Functions: SODs play a critical role in protecting cells from oxidative damage by converting superoxide radicals into hydrogen peroxide and oxygen. This process is vital for cellular defense against oxidative stress .

Role in Immune Responses and Pathogen Recognition: SODs are involved in modulating immune responses by regulating the levels of ROS, which are crucial for pathogen recognition and elimination. They help in maintaining the redox balance during immune responses .

Modes of Action

Mechanisms with Other Molecules and Cells: SODs interact with various molecules and cells to neutralize superoxide radicals. The enzyme alternates between reduced and oxidized states to facilitate the conversion of superoxide radicals into hydrogen peroxide and oxygen .

Binding Partners and Downstream Signaling Cascades: SODs bind to metal cofactors (copper, zinc, manganese, iron, or nickel) to catalyze the dismutation reaction. This process is crucial for initiating downstream signaling cascades that protect cells from oxidative damage .

Regulatory Mechanisms

Transcriptional Regulation: The expression of SOD genes is regulated by various transcription factors that respond to oxidative stress. For example, the transcription factor Nrf2 plays a significant role in upregulating SOD expression in response to increased ROS levels .

Post-Translational Modifications: SODs undergo various post-translational modifications, such as phosphorylation and acetylation, which can affect their activity and stability .

Applications

Biomedical Research: SODs are extensively studied for their role in protecting cells from oxidative damage and their potential therapeutic applications in diseases associated with oxidative stress .

Diagnostic Tools: SOD activity is used as a biomarker for oxidative stress in various diseases, including neurodegenerative disorders and cardiovascular diseases .

Therapeutic Strategies: SOD mimetics and gene therapy approaches are being developed to enhance SOD activity in conditions where oxidative stress plays a significant role .

Role in the Life Cycle

Development to Aging and Disease: SODs play a crucial role throughout the life cycle, from development to aging. They help in maintaining cellular homeostasis and protecting against age-related diseases by mitigating oxidative damage. SODs are also involved in the defense against intracellular pathogens, ensuring the survival of cells under oxidative stress .

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