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anti-Human COX4I1 Antibodies:
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Human Monoclonal COX4I1 Primary Antibody for ICC, FACS - ABIN969060
Van Kuilenburg, Van Beeumen, Demol, Van den Bogert, Schouten, Muijsers: Subunit IV of human cytochrome c oxidase, polymorphism and a putative isoform. in Biochimica et biophysica acta 1992
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Cow (Bovine) Polyclonal COX4I1 Primary Antibody for IHC, WB - ABIN2775574
Williams, Valnot, Rustin, Taanman: Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1. in The Journal of biological chemistry 2004
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Cow (Bovine) Polyclonal COX4I1 Primary Antibody for ICC, IF - ABIN258127
Zan, Zhang, Al-Qahtani, Pone, White, Lee, Yel, Mai, Casali: Endonuclease G plays a role in immunoglobulin class switch DNA recombination by introducing double-strand breaks in switch regions. in Molecular immunology 2011
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Human Polyclonal COX4I1 Primary Antibody for ICC, IF - ABIN4300196
Rice, Smith, Roberts, Perez-Costas, Melendez-Ferro: Assessment of cytochrome C oxidase dysfunction in the substantia nigra/ventral tegmental area in schizophrenia. in PLoS ONE 2014
Human Polyclonal COX4I1 Primary Antibody for IHC (p), IHC - ABIN261104
Fukuda, Zhang, Kim, Shimoda, Dang, Semenza: HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. in Cell 2007
Human Polyclonal COX4I1 Primary Antibody for FACS, IF (cc) - ABIN2173360
Wang, He, Wu, Li, Gao, Zeng: Artemisinin mimics calorie restriction to trigger mitochondrial biogenesis and compromise telomere shortening in mice. in PeerJ 2015
Human Monoclonal COX4I1 Primary Antibody for ELISA, FACS - ABIN4300195
Akimoto, Okuhira, Aizawa, Wada, Honda, Fukubayashi, Ushida: Skeletal muscle adaptation in response to mechanical stress in p130cas-/- mice. in American journal of physiology. Cell physiology 2013
We provide evidence that COX4-1 controls BMI1 (show BMI1 Antibodies) expression via a redox mechanism
COXIV mRNA (1.6 fold; P<0.01) and COXIV protein expression (1.5 fold; P<0.05) were increased by training but COXIV protein expression was decreased (20%; P<0.01) by acute exercise pre- and post-training.
Identification of three transcription factors that bind a conserved responsive element of the COX4I2 gene, namely recombination signal sequence-binding protein Jkappa (RBPJ (show RBPJ Antibodies)), coiled-coil-helix-coiled-coil-helix domain 2 (CHCHD2) and CXXC finger protein 5 (CXXC5 (show CXXC5 Antibodies)).
COX (show COX8A Antibodies) activity (electron transport complex IV) is reduced by 29% in maternal history of Alzheimer's disease compared to normal controls, and by 30% compared to paternal history of Alzheimer's disease.
Studies suggest a model that links cell signaling with the phosphorylation state of Cytochrome c (Cytc (show CYCS Antibodies)) and cytochrome c (show CYCS Antibodies) oxidase (COX (show COX8A Antibodies)).
Studies suggest that the main function of nuclear encoded subunits of cytochrome c (show CYCS Antibodies) oxidase appears to be "only" to control the activity of the mitochondrial subunits.
Studies indicate that the mechanism for proton pumping in cytochrome c (show CYCS Antibodies) oxidase is based on an electrostatic analysis of a kinetic experiment for the O to E transition.
Studies indicate that nitric oxide (NO) inhibition of cytochrome c (show CYCS Antibodies) oxidase (CcOX (show COX5A Antibodies)) is rapid and reversible and may occur in competition with oxygen.
Novel insights into the assembly and function of human nuclear-encoded cytochrome c (show CYCS Antibodies) oxidase subunits 4
Data found that subunits Cox6a (show COX6A1 Antibodies), Cox6b (show COX6B1 Antibodies) and Cox7a (show COX7A1 Antibodies) assembled into pre-existing complex IV, while Cox4-1 and Cox6c (show COX6C Antibodies) subunits assembled into subcomplexes that may represent rate-limiting intermediates.
Studies indicate that the patterns of charge translocation of cytochrome c (show CYCS Antibodies) oxidase coupled to transfer of the 3rd and 4th electrons are very similar.
Studies indicate that mutational amino acid replacement in proton channels, at the negative (N) side of membrane-inserted prokaryotic aa(3 (show ACY3 Antibodies)) oxidases, as well as Zn(2+) binding at this site in the bovine oxidase, uncouples proton pumping.
Studies indicate that nitric oxide (NO) binding to reduced ba(3) and bovine cytochrome aa3 (show ACY3 Antibodies).
Studies indicate that X-ray structure of heart cytochrome c (show CYCS Antibodies) oxidase (CcO (show RYR1 Antibodies)) suggest that O(2) molecules are transiently trapped at the Cu(B) site before binding to Fe(a3)(2+) to provide O(2)(-).
Studies indicate that photoexcitation of Ru (II) to Ru(II*) leads to rapid electron transfer to the ferric heme group in cytochrome c (show CYCS Antibodies) (Cc), followed by electron transfer to Cu(A) in cytochrome c (show CYCS Antibodies) oxidase (CcO (show RYR1 Antibodies)) with a rate constant of 60,000s(-1).
Studies suggest for the His291 model of proton pumping in cytochrome c (show CYCS Antibodies) oxidase (CcO (show RYR1 Antibodies)).
exercise training caused an increase in mRNA and protein levels of COXIV, whereas NAC (show NLRP1 Antibodies) intervention lowered the two so significantly that even exercise training could not reverse the effect of NAC (show NLRP1 Antibodies) intervention
Data suggest that that obesity affects both sperm and seminal plasma composition; Cox4i1 mRNA is up-regulated in spermatozoa of obese mice compared to control mice.
Our data suggest that MPP(+) acts on astrocytes in a sex- and brain region-specific manner involving cytochrome c (show CYCS Antibodies) oxidase isoform expression in an impairment of energy production and elevated oxidative stress levels
Knockdown of small interfering RNA-mediated COX (show CPOX Antibodies) subunit IV decreases progesterone synthesis in steroidogenic cells.
Under conditions of reduced oxygen availability, hypoxia-inducible factor 1 (show HIF1A Antibodies) reciprocally regulates COX4 subunit expression by activating transcription of the genes encoding COX4-2 and LON (show LONP1 Antibodies), a mitochondrial protease that is required for COX4-1 degradation.
Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It 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 be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.
cytochrome c oxidase subunit 4 isoform 1, mitochondrial
, OXPHOS complex IV subunit IV
, cytochrome c oxidase polypeptide IV
, cytochrome c oxidase subunit IV
, COX IV-1
, cytochrome c oxydase subunit 4
, cytochrome c oxidase, subunit IVa
, cytochrome c oxidase, subunit 4a
, cytochrome c oxidase, subunit IV
, COX IV-2
, cytochrome c oxidase subunit 4 isoform 2, mitochondrial
, cytochrome c oxidase subunit IV-like 2