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SOD-A from Bacteria

Original price was: $148.00.Current price is: $37.00.

SKU: PW14836854300 Category:

Description

SOD-A from Bacteria

Catalog number: B2014431
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 25 g
Molecular Weight or Concentration: 25.2 kDa
Supplied as: Solution
Applications: Enzymology, oxidative stress research, microbial pathogenesis studies
Storage: 20C
Keywords: MnSOD, SOD2, Superoxide dismutase, manganese, bacterial antioxidant enzyme
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 m.

SOD-A from Bacteria is a manganese-dependent superoxide dismutase (MnSOD) that plays a vital role in microbial defense against oxidative stress. With a molecular weight of ~25.2 kDa, this bacterial enzyme catalyzes the dismutation of superoxide radicals into oxygen and hydrogen peroxide, protecting cells from reactive oxygen species (ROS)-induced damage. Its role in bacterial physiology makes it an important target for studies on oxidative stress mechanisms and microbial pathogenesis.

This biotechnology-grade preparation is supplied as a ready-to-use solution, offering researchers a reliable tool for biochemical assays, enzyme kinetics, and redox biology research. SOD-A from Bacteria is especially useful in comparative enzymology, metal-specific activity investigations, and host-pathogen interaction studies where ROS signaling and defense mechanisms are central. Its stability and purity ensure reproducible results across multiple experimental applications, from enzymatic activity assays to structural biology and protein engineering research.

Key benefits:

  • Mn-dependent superoxide dismutase with defined molecular weight (25.2 kDa)

  • Neutralizes superoxide radicals, a major source of oxidative stress

  • Useful in enzymology, oxidative damage, and redox signaling research

  • Valuable for studying bacterial physiology and host-pathogen interactions

  • Biotechnology grade with 0.22 m filtration for high purity and reproducibility

  • Supplied as a 25 g solution, stored at 20C

Products are for in vitro research use only (RUO).

References

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  • Turankar RP, Pandey S, Lavania M, Singh I, Nigam A, Darlong J, Darlong F, Sengupta U. Comparative evaluation of PCR amplification of RLEP, 16S rRNA, rpoT and Sod A gene targets for detection of M. leprae DNA from clinical and environmental samples. Int J Mycobacteriol. 2015 Mar;4(1):54-9.
  • Yamakura F, Sugio S, Hiraoka BY, Ohmori D, Yokota T. Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site. Biochemistry. 2003 Sep 16;42(36):10790-9.
  • Falconi M, Iovino M, Desideri A. A model for the incorporation of metal from the copper chaperone CCS into Cu,Zn superoxide dismutase. Structure. 1999 Aug 15;7(8):903-8.
  • Schultz MJ, Haas LE. Antibiotics or probiotics as preventive measures against ventilator-associated pneumonia: a literature review. Crit Care. 2011;15(1):R18.
  • Mulyanti D, Soewandhi SN, Riani C. Insertion of prpoD_rpoS fragment enhances expression of recombinant protein by dps auto-inducible promoter in Escherichia coli. Mol Biol Rep. 2021 Aug;48(8):5833-5845.
  • Asmah RH, Sackey P, Adjei P, Archampong TN, Attoh S, Doku D, Quarchie M, Botchway F, Adedia D, Donkor ES. Haematological Indices and Antioxidant Enzyme Activity in Ghanaian Stroke Patients. Biomed Res Int. 2022 Mar 3;2022:1203120.
  • Pesci EC, Pickett CL. Genetic organization and enzymatic activity of a superoxide dismutase from the microaerophilic human pathogen, Helicobacter pylori. Gene. 1994 May 27;143(1):111-6.
  • Barrire C, Brckner R, Talon R. Characterization of the single superoxide dismutase of Staphylococcus xylosus. Appl Environ Microbiol. 2001 Sep;67(9):4096-104.