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.
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.
Purity:
> 95% as determined by reducing SDS-PAGE.
Mol Mass:
31.3 kDa
AP Mol Mass:
32 kDa
Formulation:
Lyophilized from a 0.2 µm filtered solution of PBS, 0.5mM EDTA, pH7.4.
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
system_update_altDatasheetSOD1/Superoxide Dismutase 1 Recombinant Protein SOD1 belongs to the Cu-Zn superoxide dismutase family. It binds copper and zinc ions and is one of two isozymes responsib
