||Recombinant Human full length recombinant Cox17 (Cytochrome C oxidase assembly protein) cloned from Human cDNA was expressed inE.coli. It consists of the full length apo-Human Cox172S-S with the addition of an GSFT N-terminal sequence. MW = 7.3 kDa.
||Cytochrome c oxidase copper chaperone is an enzyme that in humans is encoded by the COX17 gene. Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.
||> 95% by SDS-PAGE. The protein was observed as a single band. Cysteine alkilation with AMS monitored by MALDI-TOF show that the protein is obtained in the 2S-S form while the cysteines of the binding site are reduced.
||1.0mg at 1.0mg/ml in 50mM KH2PO4/K2HPO4 pH7, 1mM DTT (Dithiothreitol). The concentration is estimated by Bradford assay.
||Under the above described conditions, to avoid precipitation or protein dimerization, the product can be concentrated to a maximum of 1mM.
||-20°C. The protein is stable at 4°C for at least 2 weeks and at 25°C for at least several hours. After initial defrost, aliquot protein into individual tubes and refreeze at -20°C. Avoid repeated freeze/defrost cycles.