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anti-Human COX4I1 Antikörper:
anti-Mouse (Murine) COX4I1 Antikörper:
anti-Rat (Rattus) COX4I1 Antikörper:
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Human Polyclonal COX4I1 Primary Antibody für 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
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Human Monoclonal COX4I1 Primary Antibody für 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 für 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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Cow (Bovine) Polyclonal COX4I1 Primary Antibody für 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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Human Polyclonal COX4I1 Primary Antibody für 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 Monoclonal COX4I1 Primary Antibody für 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
Human Polyclonal COX4I1 Primary Antibody für 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
COX4I1 variant K101N was identified in a patient with short stature, poor weight gain and increased chromosomal breaks, simulating Fanconi anemia (zeige PALB2 Antikörper).
We provide evidence that COX4-1 controls BMI1 (zeige BMI1 Antikörper) 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.
COX (zeige COX8A Antikörper) 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 (zeige CYCS Antikörper)) and cytochrome c (zeige CYCS Antikörper) oxidase (COX (zeige COX8A Antikörper)).
Studies suggest that the main function of nuclear encoded subunits of cytochrome c (zeige CYCS Antikörper) oxidase appears to be "only" to control the activity of the mitochondrial subunits.
Studies indicate that the mechanism for proton pumping in cytochrome c (zeige CYCS Antikörper) 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 (zeige CYCS Antikörper) oxidase (CcOX (zeige COX5A Antikörper)) is rapid and reversible and may occur in competition with oxygen.
Novel insights into the assembly and function of human nuclear-encoded cytochrome c (zeige CYCS Antikörper) oxidase subunits 4
Data found that subunits Cox6a (zeige COX6A1 Antikörper), Cox6b (zeige COX6B1 Antikörper) and Cox7a (zeige COX7A1 Antikörper) assembled into pre-existing complex IV, while Cox4-1 and Cox6c (zeige COX6C Antikörper) subunits assembled into subcomplexes that may represent rate-limiting intermediates.
exercise training caused an increase in mRNA and protein levels of COXIV, whereas NAC (zeige NLRP1 Antikörper) intervention lowered the two so significantly that even exercise training could not reverse the effect of NAC (zeige NLRP1 Antikörper) 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 (zeige MPZ Antikörper)(+) acts on astrocytes in a sex- and brain region-specific manner involving cytochrome c (zeige CYCS Antikörper) oxidase isoform expression in an impairment of energy production and elevated oxidative stress levels
Knockdown of small interfering RNA-mediated COX (zeige CPOX Antikörper) subunit IV decreases progesterone synthesis in steroidogenic cells.
Under conditions of reduced oxygen availability, hypoxia-inducible factor 1 (zeige HIF1A Antikörper) reciprocally regulates COX4 subunit expression by activating transcription of the genes encoding COX4-2 and LON (zeige LONP1 Antikörper), a mitochondrial protease that is required for COX4-1 degradation.
Structure of bovine cytochrome c (zeige CYCS Antikörper) oxidase crystallized at a neutral pH has been reported.
Studies indicate that the patterns of charge translocation of cytochrome c (zeige CYCS Antikörper) 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 (zeige ACY3 Antikörper)) 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 (zeige ACY3 Antikörper).
Studies indicate that X-ray structure of heart cytochrome c (zeige CYCS Antikörper) oxidase (CcO (zeige RYR1 Antikörper)) 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 (zeige CYCS Antikörper) (Cc), followed by electron transfer to Cu(A) in cytochrome c (zeige CYCS Antikörper) oxidase (CcO (zeige RYR1 Antikörper)) with a rate constant of 60,000s(-1).
Studies suggest for the His291 model of proton pumping in cytochrome c (zeige CYCS Antikörper) oxidase (CcO (zeige RYR1 Antikörper)).
Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit IV isoform 1 of the human mitochondrial respiratory chain enzyme. It is located at the 3' of the NOC4 (neighbor of COX4) gene in a head-to-head orientation, and shares a promoter with it.
, cytochrome c oxidase polypeptide IV
, cytochrome c oxidase subunit 4 isoform 1, mitochondrial
, OXPHOS complex IV subunit IV
, cytochrome c oxidase, subunit IVa
, cytochrome c oxidase, subunit 4a
, cytochrome c oxidase, subunit IV
, cytochrome c oxydase subunit 4
, cytochrome c oxidase subunit IV
, cytochrome c oxidase IV subunit
, cytochrome c oxidase subunit IV isoform 1 S homeolog
, CG10396 gene product from transcript CG10396-RB
, cytochrome c oxidase subunit 4-like