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貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
基因功能參考文獻:
These results collectively indicate that Cox17 might not participate in the action of these anticancer organoruthenium complexes, and further verify the distinct anticancer mechanism of the organoruthenium(II) complexes from cisplatin. PMID: 27235272
Data show that the redox state of cytochrome c oxidase assembly protein 17 (Cox17), mitochondrial membrane transport protein Mia40 and superoxide dismutase 1 (SOD1) in the cytoplasm were directly observed with in-cell NMR spectroscopy. PMID: 26589182
Data suggest that Cox17 enhances the reactivity of some platinum/organoplatinum antineoplastic drugs but suppresses the reactivity of at least one platinum antineoplastic drug; glutathione modulates binding of platinum/organoplatinum drugs to Cox17. PMID: 26399480
Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective. PMID: 21816817
Data imply that up-regulation of COX17 function and increased cytochrome c oxidase activity are frequent features of lung carcinogenesis. PMID: 14612491
The binding of copper to Cox17 is needed to activate cytochrome c oxidase by Cox17. PMID: 15504366
Cox17-mediated copper metallation of Sco1, as well as the subsequent failure of Cu(A) site maturation, is the basis for the inefficient assembly of the cytochrome c oxidase complex in SCO1 patients PMID: 16520371
Cox17 was studied with regard to its expression, purification, and formation of mixed disulfide adducts with sulfhydryl reagents. PMID: 17208454
XAS (X-ray absorption spectroscopy) determined that Cu4Cox17 contains a Cu4S6-type copper-thiolate cluster, which may provide safe storage of an excess of copper ions PMID: 17672825
Cu(I)HCox17(2S-S), i.e., the copper-loaded form of the protein, can transfer simultaneously copper(I) and two electrons to the human cochaperone Sco1 (HSco1) in the oxidized state, i.e., with its metal-binding cysteines forming a disulfide bond. PMID: 18458339
the absence of Cox17 interferes with copper delivery to Cox2, but not to Cox1. PMID: 19393246