SCO1 Antibody

1. Results find that COA6 associates with COX2 and is crucial for its maturation and complex IV biogenesis. Also, COA6 interacts with the copper chaperone SCO1 which indicates that COA6 is intrinsically involved in the copper delivery process for COX2. PMID: 26160915
2. Sco1 is a metallochaperone that selectively transfers Cu(I) ions based on loop recognition, whereas Sco2 is a copper-dependent thiol reductase of the cysteine ligands in the oxidase. PMID: 26351686
3. COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the assembly of cytochrome c oxidase. PMID: 24403053
4. COX19 is necessary for the transduction of a SCO1-dependent mitochondrial redox signal that regulates ATP7A-mediated cellular copper efflux. PMID: 23345593
5. Results describe the tissue distribution of SCO1 and SCO2 in mouse and human tissues. PMID: 20864674
6. SCO1 facilitates the transfer of copper from SCO2 to the CuA site at an early stage of COX assembly in mitochondria. PMID: 15229189
7. data suggest that both Cu(I) and Cu(II) binding are critical for normal Sco function. PMID: 16091356
8. 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
9. Sco1 has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function. PMID: 16735468
10. These results suggest a mitochondrial pathway for the regulation of cellular copper content that involves signaling through SCO1 and SCO2, perhaps by their thiol redox or metal-binding state. PMID: 17189203
11. 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
12. a fraction of Sco1 physically associates with the cytochrome c oxidase complex in human muscle mitochondria, suggesting a possible direct relationship between CcO and the regulation of cellular copper homeostasis PMID: 19295170
13. SCO2 acts upstream of SCO1, and that it is indispensable for CO II synthesis. PMID: 19336478

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HGNC: 10603

OMIM: 220110

KEGG: hsa:6341

STRING: 9606.ENSP00000255390

UniGene: Hs.14511