COX4I1 & COX4I2
- Known as:
- COX4I1 & COX4I2
- Catalog number:
- Y213666
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- COX4I1 & COX4I2
Related genes to: COX4I1 & COX4I2
- Gene:
- COX4I1 NIH gene
- Name:
- cytochrome c oxidase subunit 4I1
- Previous symbol:
- COX4
- Synonyms:
- COX4-1
- Chromosome:
- 16q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-02-11
- Gene:
- COX4I2 NIH gene
- Name:
- cytochrome c oxidase subunit 4I2
- Previous symbol:
- COX4L2
- Synonyms:
- COXIV-2, COX4B, dJ857M17.2, COX4-2
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-03
- Date modifiied:
- 2016-02-11
Related products to: COX4I1 & COX4I2
anti-COX4I1 (6B3)anti-COX4I1 (C-Terminus)Anti-COX4I1, Goat Polyclonal to COX4I1, Isotype , Host Goatanti-COX4I2 (aa31-80)Antibodies: COX4I1 & COX4I2 HOST: Goat Clonality: pAbAntibodies: COX4I2 & COX4I1 HOST: Goat Clonality: pAbBos taurus,Bovine,COX IV-1,COX4,COX4I1,Cytochrome c oxidase polypeptide IV,Cytochrome c oxidase subunit 4 isoform 1, mitochondrial,Cytochrome c oxidase subunit IV isoform 1Bovine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial(COX4I1) ELISA kitBovine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial(COX4I1) ELISA kitBovine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial(COX4I1) ELISA kit SpeciesBovineBovine Cytochrome c oxidase subunit 4 isoform 2, mitochondrial(COX4I2) ELISA kitBovine cytochrome c oxidase subunit IV isoform 1 (COX4I1) ELISA kit, Species Bovine, Sample Type serum, plasmaCanine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial(COX4I1) ELISA kitCanine Cytochrome c oxidase subunit 4 isoform 1, mitochondrial(COX4I1) ELISA kitCanine Cytochrome c oxidase subunit 4 isoform 2, mitochondrial(COX4I2) ELISA kit Related articles to: COX4I1 & COX4I2
- The conditions of hypoxia are suggested to induce permanent atrial fibrillation (AF). The regulation of COX4I2 and COX4I1 depends on oxygen availability in tissues. A role of COX4I2 in the myocardium of AF patients is supposed for pathogenesis of AF and subsequent alterations in the electron transfer chain (ETC) under hypoxia. - Source: PubMed
Publication date: 2023/12/27
Vogt SebastianRamzan RabiaCybulski PiaRhiel AnnikaWeber PetraRuppert VolkerIrqsusi MarcRohrbach SusanneNiemann BerndMirow NikolasRastan Ardawan J - Astaxanthin is gaining recognition as a natural bioactive component. This study aimed to test whether astaxanthin could protect adipose-derived stromal stem cells (ASCs) from apoptosis, mitochondrial dysfunction and oxidative stress. was used to extract astaxanthin, whose biocompatibility was tested after 24, 48 and 72 h of incubation with the cells; no harmful impact was found. ASCs were treated with optimal concentrations of astaxanthin. Several parameters were examined: cell viability, apoptosis, reactive oxygen levels, mitochondrial dynamics and metabolism, superoxide dismutase activity, and astaxanthin's antioxidant capacity. A RT PCR analysis was performed after each test. The astaxanthin treatment significantly reduced apoptosis by modifying the normalized caspase activity of pro-apoptotic pathways (p21, p53, and Bax). Furthermore, by regulating the expression of related master factors SOD1, SOD2, PARKIN, PINK 1, and MFN 1, astaxanthin alleviated the oxidative stress and mitochondrial dynamics failure caused by EMS. Astaxanthin restored mitochondrial oxidative phosphorylation by stimulating markers associated with the OXPHOS machinery: COX4I1, COX4I2, UQCRC2, NDUFA9, and TFAM. Our results suggest that astaxanthin has the potential to open new possibilities for potential bio-drugs to control and suppress oxidative stress, thereby improving the overall metabolic status of equine ASCs suffering from metabolic syndrome. - Source: PubMed
Publication date: 2022/07/27
Mularczyk MalwinaBourebaba NabilaMarycz KrzysztofBourebaba Lynda - Cytochrome--oxidase (COX) subunit 4 (COX4) plays important roles in the function, assembly and regulation of COX (mitochondrial respiratory complex 4), the terminal electron acceptor of the oxidative phosphorylation (OXPHOS) system. The principal COX4 isoform, COX4-1, is expressed in all tissues, whereas COX4-2 is mainly expressed in the lungs, or under hypoxia and other stress conditions. We have previously described a patient with a COX4-1 defect with a relatively mild presentation compared to other primary COX deficiencies, and hypothesized that this could be the result of a compensatory upregulation of COX4-2. To this end, COX4-1 was downregulated by shRNAs in human foreskin fibroblasts (HFF) and compared to the patient's cells. COX4-1, COX4-2 and HIF-1α were detected by immunocytochemistry. The mRNA transcripts of both COX4 isoforms and HIF-1 target genes were quantified by RT-qPCR. COX activity and OXPHOS function were measured by enzymatic and oxygen consumption assays, respectively. Pathways were analyzed by CEL-Seq2 and by RT-qPCR. We demonstrated elevated COX4-2 levels in the COX4-1-deficient cells, with a concomitant HIF-1α stabilization, nuclear localization and upregulation of the hypoxia and glycolysis pathways. We suggest that COX4-2 and HIF-1α are upregulated also in normoxia as a compensatory mechanism in COX4-1 deficiency. - Source: PubMed
Publication date: 2021/02/20
Douiev LizaMiller ChayaRuppo ShmuelBenyamini HadarAbu-Libdeh BassamSaada Ann - This study identified the changes in hypertrophy/atrophy and mitochondrial-related signaling in human skeletal muscle following whole-body (WB) and localized single leg (SL) heat treatment. Nine active male participants were administered either 60 min of passive WB (44-50°C, 50% humidity) or SL (water-perfused suit at 49.5 ± 1.4°C) heat treatment at least 1 week apart in a counterbalanced order. The untreated leg during SL was considered as control (CON). Core, skin, and quadriceps muscle temperature were monitored throughout the experimental trials. Muscle microbiopsy samples were obtained prior to (PRE), and 30 min and 3 h post (POST) following heat treatment. Muscle temperature increased with time ( < 0.0001) in both WB and SL, with no differences between conditions (38.8 ± 0.5°C vs. 38.1 ± 0.6°C, = 0.065). Core temperature increased only following WB, and was significantly higher compared with SL (39.1 ± 0.3°C vs. 37.1 ± 0.1, < 0.0001). Compared with PRE, WB up-regulated the phosphorylation status of the majority of the Akt/mTOR pathway (Akt, mTOR, S6K1, rpS6, and p-eIF4E; ≤ 0.050), with the exception of 4EBP1 ( = 0.139). WB also increased the mRNA of HSPs 72, 90, and 25 (all < 0.021), and increased or tended to increase the phosphorylation of FOXO1 ( = 0.066) and FOXO3a ( = 0.038). In addition, most (NRF1, NRF2, COX2, and COX4-I2; all ≤ 0.050), but not all (CS, Cyt c, and COX4-I1; > 0.441) mRNA content indicative of mitochondrial biogenesis were increased following WB, with no changes evident in these parameters in SL or CON (all > 0.090). These results indicate that 1 h of WB heat treatment enhanced anabolic (Akt/mTOR), mitochondrial, and cyto-protective signaling (HSP), with a concomitant possible inhibition of FOXO transcription factors. - Source: PubMed
Publication date: 2020/07/14
Ihsan MohammedDeldicque LouiseMolphy JohnBritto FlorianCherif AnissaRacinais Sebastien - Cytochrome oxidase (COX) is regulated through tissue-, development- or environment-controlled expression of subunit isoforms. The COX4 subunit is thought to optimize respiratory chain function according to oxygen-controlled expression of its isoforms COX4i1 and COX4i2. However, biochemical mechanisms of regulation by the two variants are only partly understood. We created an HEK293-based knock-out cellular model devoid of both isoforms (COX4i1/2 KO). Subsequent knock-in of COX4i1 or COX4i2 generated cells with exclusive expression of respective isoform. Both isoforms complemented the respiratory defect of COX4i1/2 KO. The content, composition, and incorporation of COX into supercomplexes were comparable in COX4i1- and COX4i2-expressing cells. Also, COX activity, cytochrome affinity, and respiratory rates were undistinguishable in cells expressing either isoform. Analysis of energy metabolism and the redox state in intact cells uncovered modestly increased preference for mitochondrial ATP production, consistent with the increased NADH pool oxidation and lower ROS in COX4i2-expressing cells in normoxia. Most remarkable changes were uncovered in COX oxygen kinetics. The p (partial pressure of oxygen at half-maximal respiration) was increased twofold in COX4i2 versus COX4i1 cells, indicating decreased oxygen affinity of the COX4i2-containing enzyme. Our finding supports the key role of the COX4i2-containing enzyme in hypoxia-sensing pathways of energy metabolism. - Source: PubMed
Publication date: 2020/02/14
Pajuelo Reguera DavidČunátová KristýnaVrbacký MarekPecinová AlenaHouštěk JosefMráček TomášPecina Petr