Recombinant Dechloromonas aromatica Chlorite Dismutase Protein (His Tag) | PKSQ050054

Recombinant Dechloromonas aromatica Chlorite Dismutase Protein (His Tag) | PKSQ050054 | Gentaur US, UK & Europe Disrtribition

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

Active Protein: N/A

Activity: Recombinant Dechloromonas aromatica Chlorite dismutase is produced by our E.coli expression system and the target gene encoding Met35-Asp282 is expressed with a 6His tag at the N-terminus.

Protein Construction: Recombinant Dechloromonas aromatica Chlorite dismutase is produced by our E.coli expression system and the target gene encoding Met35-Asp282 is expressed with a 6His tag at the N-terminus.

Fusion Tag: N-His

Species: Dechloromonas aromatica

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 31.3 kDa

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.

Research Area: N/A