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Human Polyclonal SCO1 Primary Antibody für IHC, ELISA - ABIN1003126
Glerum, Shtanko, Tzagoloff: SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. in The Journal of biological chemistry 1996
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Human Polyclonal SCO1 Primary Antibody für IHC (p), WB - ABIN541294
Horng, Leary, Cobine, Young, George, Shoubridge, Winge: Human Sco1 and Sco2 function as copper-binding proteins. in The Journal of biological chemistry 2005
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Human Polyclonal SCO1 Primary Antibody für ICC, IF - ABIN4352258
Rolland, Motori, Memar, Hench, Frank, Winklhofer, Conradt: Impaired complex IV activity in response to loss of LRPPRC function can be compensated by mitochondrial hyperfusion. in Proceedings of the National Academy of Sciences of the United States of America 2013
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.
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.
COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the assembly of cytochrome c oxidase.
COX19 is necessary for the transduction of a SCO1-dependent mitochondrial redox signal that regulates ATP7A-mediated cellular copper efflux.
Results describe the tissue distribution of SCO1 and SCO2 in mouse and human tissues.
SCO1 facilitates the transfer of copper from SCO2 to the CuA site at an early stage of COX assembly in mitochondria.
data suggest that both Cu(I) and Cu(II) binding are critical for normal Sco function.
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
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.
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.
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.
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
SCO2 acts upstream of SCO1, and that it is indispensable for CO II synthesis.
Mammalian cytochrome c oxidase (COX) catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. In yeast, 2 related COX assembly genes, SCO1 and SCO2 (synthesis of cytochrome c oxidase), enable subunits 1 and 2 to be incorporated into the holoprotein. This gene is the human homolog to the yeast SCO1 gene.
SCO cytochrome oxidase deficient homolog 1
, protein SCO1 homolog, mitochondrial
, SCO cytochrome oxidase deficient homolog 1 (yeast)