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AB110271

Anti-MTCO2 抗体 [4B12A5]

Anti-MTCO2 antibody [4B12A5]

1

(1 Review)

|

(45 Publications)

Mouse Monoclonal MTCO2 antibody. Suitable for WB and reacts with Saccharomyces cerevisiae samples. Cited in 45 publications.

別名を表示する

OXI1, Q0250, COX2, Cytochrome c oxidase subunit 2, Cytochrome c oxidase polypeptide II

2 Images
Western blot - Anti-MTCO2 antibody [4B12A5] (AB110271)
  • WB

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Western blot - Anti-MTCO2 antibody [4B12A5] (AB110271)

All lanes:

Western blot - Anti-MTCO2 antibody [4B12A5] (ab110271) at 2 µg/mL

All lanes:

Mitochondria from yeast membrane extract at 10 µg

Predicted band size: 25 kDa

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Western blot - Anti-MTCO2 antibody [4B12A5] (AB110271)
  • WB

CiteAb

Western blot - Anti-MTCO2 antibody [4B12A5] (AB110271)

MTCO2 western blot using anti-MTCO2 antibody [4B12A5] ab110271. Publication image and figure legend from de Taffin de Tilques, M., Tribouillard-Tanvier, D., et al., 2017, Dis Model Mech, PubMed 28188263.

ab110271 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab110271 please see the product overview.

BN-PAGE and SDS-PAGE analyses of mitochondrial proteins. Experiments were performed with mitochondria isolated from strains WT+pØ, taz1Δ+pØ, taz1Δ+pTAZ1 and taz1Δ+pODC1 grown as described in Fig. 2B. (A) BN-PAGE analyses of ATP synthase. The left panel shows a BN-gel of mitochondrial proteins (50 µg) dissolved with 2 g of digitonin per g of proteins, where ATP synthase is revealed by its ATPase activity as dimers (V2), monomers (V1) or free F1 particles (F1). In the right panel, ATP synthase was analyzed in samples (50 µg) obtained after treating the mitochondria with increasing concentrations of digitonin, from 0.5 to 3.0 g per g of protein. After their electrophoretic separation and transfer onto a nitrocellulose membrane, the proteins were probed with antibodies against the γ-F1 subunit (ATP3) of ATP synthase. (B) BN-PAGE analysis of CIV and CIII. Mitochondrial proteins were extracted with 10 g digitonin per g of protein, separated by BN-PAGE (100 µg per lane), transferred onto a nitrocellulose membrane, and probed with antibodies against the COX2 subunit of CIV or the cytochrome b subunit of CIII. (C) BN-PAGE and SDS-PAGE analyses of CII. On the left panel, mitochondrial proteins were extracted with digitonin (10 g/g), separated by BN-PAGE, and assayed for in-gel complex II activity; in the right panel, 100 µg of total protein extracts were separated by SDS-PAGE, transferred onto a nitrocellulose membrane and probed antibodies against SDH2 and ADE13. (D) SDS-PAGE analyses. 100 µg of total mitochondrial proteins were separated by SDS-PAGE, transferred onto a nitrocellulose membrane and probed with antibodies against the indicated proteins. The right panel shows a quantification which as been done using ImageJ. Levels of COX2, ATPα-F1 and cytochrome c are related to the mitochondrial protein Por1p. The data are all relative to WT.

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Key facts

宿主種

Mouse

クローン性

Monoclonal

クローン番号

4B12A5

アイソタイプ

IgG2a

軽鎖のタイプ

kappa

キャリアフリー

No

交差種

Saccharomyces cerevisiae

アプリケーション

WB

applications

免疫原

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Saccharomyces cerevisiae": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "2 µg/mL", "WB-species-notes": "<p></p>" } } }

製品の詳細

Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com

出荷温度及び保存条件

製品の状態
Liquid
精製度
IgG fraction
精製に関する特記事項
Near homogeneity as judged by SDS-PAGE. ab110271 was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation.
バッファー組成
pH: 7.5 Preservative: 0.02% Sodium azide Constituents: HEPES buffered saline
出荷温度
Blue Ice
短期保存温度
+4°C
長期保存温度
+4°C
保管に関する情報
Do Not Freeze

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

'MTCO2' also known as 'mt-co2' or 'mtco2e' is a mitochondrial gene that encodes for a component of the cytochrome c oxidase complex referred to as Complex IV in the electron transport chain. The protein plays a mechanical role in facilitating electron transfer within mitochondria an essential process in cellular respiration. MTCO2 is predominantly expressed in tissues with high energy demands such as muscle and neurons. The known mass of the MTCO2 protein is approximately 25 kDa. It sits in the mitochondrial inner membrane where it contributes to creating the proton gradient driving ATP synthesis.
Biological function summary

MTCO2 (or cytochrome c oxidase subunit II) serves as an important player in aerobic respiration. It is part of the cytochrome c oxidase complex which forms the last enzyme complex of the electron transport chain. As part of this complex MTCO2 facilitates the transfer of electrons from cytochrome c to oxygen resulting in the reduction of oxygen to water. This electron transfer is paired with proton translocation across the mitochondrial membrane which is critical for ATP production.

Pathways

MTCO2 contributes significantly to the oxidative phosphorylation pathway which is essential for ATP production in eukaryotic cells. It directly interacts with other components of the mitochondrial electron transport chain like cytochrome c and NADH dehydrogenase which are critical for maintaining the flow of electrons and the integrity of the energy production process. Another pathway it is part of is the apoptosis pathway regulated by non-lethal stress conditions where controlled release of cytochrome c can trigger programmed cell death.

MTCO2 mutations and dysfunctions have been linked with mitochondrial disorders especially those affecting energy-demanding tissues leading to conditions such as mitochondrial myopathy and Leber's hereditary optic neuropathy. These disorders result from compromised oxidative phosphorylation leading to inadequate energy supply. The dysfunction of cytochrome c oxidase which contains the MTCO2 subunit is a central aspect of these diseases often tying this protein to other complexes within the electron transport chain that also underpin mitochondrial diseases.

製品プロトコール

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ターゲットの情報

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX2 is a catalytic core subunit which transfers the electrons from cytochrome c via its dinuclear copper A center (CU(A)) to the BNC of the COX1 (PubMed : 30598554).
See full target information COX2

文献 (45)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 16:5314 PubMed40595511

2025

A constricted mitochondrial morphology formed during respiration.

Applications

Unspecified application

Species

Unspecified reactive species

Manish K Singh,Laetitia Cavellini,Maria Angeles Morcillo-Parra,Christina Kunz,Mickaël Lelek,Perrine Bomme,Aurélia Barascu,Cynthia Alsayyah,Maria Teresa Teixeira,Naïma Belgareh-Touzé,Adeline Mallet,Lea Dietrich,Christophe Zimmer,Mickael M Cohen

Genetics 229: PubMed40178993

2025

A new set of mutations in the second transmembrane helix of the Cox2p-W56R substantially improves its allotopic expression in Saccharomyces cerevisiae.

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Unspecified application

Species

Unspecified reactive species

Kewin Gombeau,Stefan A Hoffmann,Yizhi Cai

Scientific reports 14:31017 PubMed39730600

2024

PCNA and Rnh1 independently participate in the protection of mitochondrial genome against UV-induced mutagenesis in yeast cells.

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Martyna Latoszek,Katarzyna Baginska-Drabiuk,Ewa Sledziewska-Gojska,Aneta Kaniak-Golik

The Journal of biological chemistry 300:107314 PubMed38657861

2024

The role of histone H3 leucine 126 in fine-tuning the copper reductase activity of nucleosomes.

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Nataliya P Tod,Maria Vogelauer,Chen Cheng,Ansar Karimian,Stefan Schmollinger,Dimitrios Camacho,Siavash K Kurdistani

Nature communications 15:1454 PubMed38365818

2024

A system for inducible mitochondria-specific protein degradation in vivo.

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Swastika Sanyal,Anna Kouznetsova,Lena Ström,Camilla Björkegren

Archives of biochemistry and biophysics 744:109665 PubMed37348627

2023

Evidence that the catalytic mechanism of heme a synthase involves the formation of a carbocation stabilized by a conserved glutamate.

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Elise D Rivett,Hannah G Addis,Jonathan V Dietz,Jayda A Carroll-Deaton,Shipra Gupta,Koji L Foreman,Minh Anh Dang,Jennifer L Fox,Oleh Khalimonchuk,Eric L Hegg

Journal of cell science 135: PubMed36185004

2022

Loss of Num1-mediated cortical dynein anchoring negatively impacts respiratory growth.

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Species

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Antoineen J White,Clare S Harper,Erica M Rosario,Jonathan V Dietz,Hannah G Addis,Jennifer L Fox,Oleh Khalimonchuk,Laura L Lackner

Journal of cell science 135: PubMed34854901

2022

Peroxisomal support of mitochondrial respiratory efficiency promotes ER stress survival.

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Imadeddin Hijazi,Emily Wang,Michelle Orozco,Sarah Pelton,Amy Chang

Redox biology 46:102125 PubMed34517185

2021

Mitochondrial contact site and cristae organizing system (MICOS) machinery supports heme biosynthesis by enabling optimal performance of ferrochelatase.

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Jonathan V Dietz,Mathilda M Willoughby,Robert B Piel,Teresa A Ross,Iryna Bohovych,Hannah G Addis,Jennifer L Fox,William N Lanzilotta,Harry A Dailey,James A Wohlschlegel,Amit R Reddi,Amy E Medlock,Oleh Khalimonchuk

PloS one 15:e0243489 PubMed33370314

2020

The plasticity of the pyruvate dehydrogenase complex confers a labile structure that is associated with its catalytic activity.

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Unspecified application

Species

Unspecified reactive species

Jaehyoun Lee,Seunghee Oh,Saikat Bhattacharya,Ying Zhang,Laurence Florens,Michael P Washburn,Jerry L Workman
View all publications

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