SOD Human

Superoxide Dismutase Human Recombinant
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Description

Catalytic Mechanism and Kinetic Efficiency

SOD catalyzes the disproportionation of superoxide via a two-step redox cycle:

Step 1: M(n+1)+-SOD+O2Mn+-SOD+O2Step 2: Mn+-SOD+O2+2H+M(n+1)+-SOD+H2O2\begin{align*} \text{Step 1: } & \text{M}^{(n+1)+}\text{-SOD} + \text{O}_2^{- -} \rightarrow \text{M}^{n+}\text{-SOD} + \text{O}_2 \\ \text{Step 2: } & \text{M}^{n+}\text{-SOD} + \text{O}_2^{- -} + 2\text{H}^+ \rightarrow \text{M}^{(n+1)+}\text{-SOD} + \text{H}_2\text{O}_2 \end{align*}

For Cu/Zn-SOD1, copper alternates between Cu²⁺ (oxidized) and Cu⁺ (reduced) states . SOD enzymes exhibit near-perfect catalytic efficiency (kcat/KM7×109M1s1k_{cat}/K_M \approx 7 \times 10^9 \, \text{M}^{-1}\text{s}^{-1}), operating at diffusion-limited rates .

Neurodegenerative Diseases

  • Amyotrophic Lateral Sclerosis (ALS): Over 170 SOD1 mutations (e.g., A4V, G93A) cause familial ALS via toxic gain-of-function mechanisms, not loss of enzymatic activity . Transgenic mice expressing mutant SOD1 develop motor neuron degeneration resembling ALS .

  • Alzheimer’s and Parkinson’s Diseases: Reduced SOD activity correlates with oxidative damage in neurodegenerative pathways .

Systemic Disorders

  • COVID-19 Severity: SOD activity decreases significantly in Omicron-variant infections, with severe cases showing the lowest levels (ROC AUC = 0.89 for mortality prediction) .

  • Cancer: SOD2 knockout mice develop hepatocellular carcinoma, while SOD1 deficiency accelerates tumorigenesis in aging models .

Experimental Therapeutics

  • SOD Mimetics: MnTnBuOE-2-PyP⁵⁺ enhances TRAIL-induced apoptosis in glioblastoma .

  • Gene Therapy: Adenoviral SOD2 delivery reduces ischemia-reperfusion injury in cardiac tissue .

Clinical Correlations

ConditionSOD AlterationClinical ImpactSource
Familial ALSSOD1 mutations (e.g., A4V)Motor neuron degeneration
COVID-19↓ SOD activity (Omicron variant)↑ Inflammation, organ injury
Rheumatoid ArthritisSOD3 deficiency↑ Joint inflammation
Age-Related CataractsSOD1 polymorphismsOxidative lens damage

Diagnostic Reference Intervals

Age- and sex-specific reference ranges for serum SOD activity in Iranian adults (35–65 years):

ParameterMales (U/mL)Females (U/mL)
SOD Activity4.79–5.124.99–5.31
Copper (µg/dL)85.7–140.392.8–157.8
Zinc (µg/dL)70.5–121.272.6–126.4

These values aid in assessing oxidative stress in conditions like diabetes and Hashimoto’s thyroiditis .

Research Challenges and Future Directions

While SOD supplementation shows promise in cystic fibrosis and radiation-induced fibrosis , limitations include short plasma half-life and immunogenicity. Conjugation with polyethylene glycol (PEG) or encapsulation in liposomes improves bioavailability . Current studies focus on SOD mimetics targeting mitochondrial ROS in neurodegenerative diseases .

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. This enzyme plays a crucial role in maintaining the balance of oxygen radicals in the body. Mutations in SOD1 are linked to a familial form of amyotrophic lateral sclerosis.
Description

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.

Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The product is provided as a lyophilized powder, obtained by freeze-drying a 0.2µm filtered solution with a concentration of 1mg/ml in phosphate-buffered saline (PBS) at pH 7.4.
Solubility
To reconstitute the lyophilized SOD, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a minimum concentration of 100µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized SOD is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store the desiccated product below -18°C. After reconstitution, SOD should be stored at 4°C for up to 7 days. For extended storage, freeze the solution below -18°C. Avoid repeated freeze-thaw cycles. The addition of a carrier protein, such as 0.1% HSA or BSA, is recommended for long-term storage.
Purity

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.

Biological Activity

The biological activity of the product, measured using the Pyrogallic Acid method, is greater than 3,000 Units/mg.

Synonyms
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
Source
Escherichia Coli.
Amino Acid Sequence

ATKAVCVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEF GDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH CIIGRTLVVH EKADDLGKGG NEESTKTGNA GSRLACGVIG IAQ.

Product Science Overview

Types and Functions of SOD

There are three main types of SOD in mammals:

  1. Cu/Zn-SOD (SOD1): Found in the cytosol, mitochondrial intermembrane space, and nucleus.
  2. Mn-SOD (SOD2): Located in the mitochondrial matrix.
  3. 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)

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 .

Production and Purification

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 .

Applications of rhSOD
  1. 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 .
  2. 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 .
  3. Food Industry: rhSOD is utilized in the food industry to enhance the shelf life of products by preventing oxidative spoilage .
Challenges and Future Directions

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.

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