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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
Show all 4 Pubmed References
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 (zeige COX2 Antikörper) 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 (zeige COX2 Antikörper).
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 (zeige SCO2 Antikörper) to mature COX2 (zeige COX2 Antikörper) and promote the assembly of cytochrome c (zeige CYCS Antikörper) oxidase.
COX19 (zeige COX19 Antikörper) is necessary for the transduction of a SCO1-dependent mitochondrial redox signal that regulates ATP7A (zeige ATP7A Antikörper)-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 (zeige SCO2 Antikörper) to the CuA site at an early stage of COX (zeige COX8A Antikörper) assembly in mitochondria.
data suggest that both Cu(I) and Cu(II) binding are critical for normal Sco (zeige SNAI1 Antikörper) 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 (zeige DNAJC5 Antikörper) motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin (zeige TXN Antikörper) 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.
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)