Recombinant Dechloromonas aromatica Chlorite Dismutase Protein (His Tag)

    • Recombinant Dechloromonas aromatica Chlorite Dismutase Protein (N-His)-Elabscience
    • Recombinant Protein-Elabscience
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    • Recombinant Dechloromonas aromatica Chlorite Dismutase Protein (N-His)-Elabscience
    • Recombinant Protein-Elabscience
    • Recombinant Dechloromonas aromatica Chlorite Dismutase Protein (N-His)-Elabscience
    • Recombinant Protein-Elabscience

      Catalog number:PKSQ050054

      Synonyms:Chlorite dismutase; Chlorite O(2)-lyase; Daro_2580; Cld

      Size:
      • 10μg
      • 50μg
      Qty:
      - +
      Price: $129

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      Overview

      Synonyms Chlorite dismutase; Chlorite O(2)-lyase; Daro_2580; Cld
      Species Dechloromonas aromatica
      Expression_host E.coli
      Sequence Met35-Asp282
      Accession Q47CX0
      Mol_Mass 31.3 kDa
      AP_Mol_Mass 32 kDa
      Tag N-His

      Properties

      Purity > 95% as determined by reducing SDS-PAGE.
      Endotoxin < 1.0 EU per μg as determined by the LAL method.
      Storage Lyophilized protein should be stored at < -20℃, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7℃ for 2-7 days.Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
      Shipping This product is provided as lyophilized powder which is shipped with ice packs.
      Formulation Lyophilized from a 0.2 μm filtered solution of PBS, 0.5mM EDTA, pH7.4.
      Reconstitution Please refer to the printed manual for detailed information.

      Background

      Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyzes the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.

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