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AB110261

Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker

3

(2 Reviews)

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(53 Publications)

Mouse Monoclonal COX IV antibody. Suitable for WB, Flow Cyt, ICC/IF, IHC-Fr and reacts with Cow, Human samples. Cited in 53 publications.

View Alternative Names

COX4, COX4I1, Cytochrome c oxidase polypeptide IV, Cytochrome c oxidase subunit IV isoform 1, COX IV-1, COX4L2, COX4I2, Cytochrome c oxidase subunit IV isoform 2, COX IV-2

5 Images
Immunocytochemistry/ Immunofluorescence - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)

ab110261, at 10 µg/ml, staining COX4 + COX4L2 in cultured Human embryonic lung derived fibroblasts by Immunofluorescence. The cells (strain MRC5) were fixed, permeabilized and then labeled with ab110261 followed by an AlexaFluor® 488 conjugated Goat anti-mouse IgG2a isotype specific secondary antibody at 1 µg/ml.

Immunohistochemistry (Frozen sections) - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)
  • IHC-Fr

Unknown

Immunohistochemistry (Frozen sections) - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)

ab110261, at 1/800, staining COX4 + COX4L2 in skeletal muscle tissue sections from a patient with a single large deletion of the mtDNA by Immunohistochemistry. The tissue was snap frozen and fixed in 4% PFA. Image kindly provided by Dr. J. Murphy and D. Turnbull, Mitochondrial Research Group, Newcastle University.

Flow Cytometry - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)
  • Flow Cyt

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Flow Cytometry - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)

ab110261, at 1 µg/mL, staining COX4 + COX4L2 in HeLa cells by Immunohistochemistry (blue) and an isotype control antibody, at 1 µg/mL, staining of HeLa cells (red).

Immunohistochemistry (Frozen sections) - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)
  • IHC-Fr

Unknown

Immunohistochemistry (Frozen sections) - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)

ab110261, at 1/200, showing COX4 + COX4L2 negative crypts in colon tissue sections from a normal ageing patient by Immunohistochemistry. The tissue was snap frozen and fixed in 4% PFA. Image kindly provided by Dr. J. Murphy and D. Turnbull, Mitochondrial Research Group, Newcastle University.

Western blot - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)
  • WB

Unknown

Western blot - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (AB110261)

All lanes:

Western blot - Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker (ab110261) at 1 µg/mL

Lane 1:

Isolated mitochondria from Human heart at 5 µg

Lane 2:

Isolated mitochondria from Bovine heart at 1 µg

Lane 3:

Isolated mitochondria from HepG2 at 20 µg

Predicted band size: 20 kDa

false

  • 519 Alexa Fluor® 488

    Alexa Fluor® 488 Anti-COX4 + COX4L2 antibody [10G8D12C12] - Mitochondrial Marker

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

10G8D12C12

Isotype

IgG2a

Light chain type

kappa

Carrier free

No

Reacts with

Cow, Human

Applications

Flow Cyt, IHC-Fr, WB, ICC/IF

applications

Immunogen

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

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Reactivity data

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Product details

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
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Properties and storage information

Form
Liquid
Purity
IgG fraction
Purification notes
ab110261 was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation. ab110261 was judged as near homogeneity by SDS PAGE.
Storage buffer
pH: 7.5 Preservative: 0.02% Sodium azide Constituents: HEPES buffered saline
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
Do Not Freeze
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Supplementary information

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

The COX4 protein also known as Cytochrome c oxidase subunit 4 along with its isoform COX4L2 forms part of the electron transport chain in mitochondria. COX4 has a molecular mass of approximately 20.8 kDa and is found in various tissues especially in high-energy-demand organs like the heart and liver. Both COX4 and COX4L2 belong to the inner mitochondrial membrane and play a role in the enzyme complex Cytochrome c oxidase essential for efficient cellular respiration.
Biological function summary

COX4 and COX4L2 contribute to the terminal stage of the mitochondrial electron transport chain. They form core components of the Cytochrome c oxidase complex also called complex IV which facilitates the transfer of electrons from reduced cytochrome c to oxygen. This process not only aids in the production of water but also helps create the proton gradient used by ATP synthase to generate ATP the primary energy currency in cells.

Pathways

Both COX4 and COX4L2 integrate into key metabolic pathways such as oxidative phosphorylation and the respiratory chain. Their role in the electron transport chain connects them to other mitochondrial proteins like cytochrome c and ATP synthase. This collaboration is important for the efficient conversion of nutrients into usable cellular energy supporting essential metabolic functions.

Disruptions in the function of COX4 and COX4L2 relate to conditions such as mitochondrial myopathy and Leigh syndrome. Mutations or deficiencies in these proteins can impair electron transport and reduce ATP generation leading to muscle weakness or neurodegenerative symptoms. Cytochrome c and other components of the electron transport chain often exhibit related dysfunctions in these mitochondrial diseases.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

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 subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
See full target information COX4I1

Additional targets

COX4I2
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Publications (53)

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

Biochimica et biophysica acta. Molecular basis of disease 1870:167131 PubMed38521420

2024

A stagewise response to mitochondrial dysfunction in mitochondrial DNA maintenance disorders.

Applications

Unspecified application

Species

Unspecified reactive species

Amy E Vincent,Chun Chen,Tiago Bernardino Gomes,Valeria Di Leo,Tuomas Laalo,Kamil Pabis,Rodrick Capaldi,Michael F Marusich,David McDonald,Andrew Filby,Andrew Fuller,Diana Lehmann Urban,Stephan Zierz,Marcus Deschauer,Doug Turnbull,Amy K Reeve,Conor Lawless

Frontiers in cell and developmental biology 10:786268 PubMed35300415

2022

Applying Sodium Carbonate Extraction Mass Spectrometry to Investigate Defects in the Mitochondrial Respiratory Chain.

Applications

Unspecified application

Species

Unspecified reactive species

David R L Robinson,Daniella H Hock,Linden Muellner-Wong,Roopasingam Kugapreethan,Boris Reljic,Elliot E Surgenor,Carlos H M Rodrigues,Nikeisha J Caruana,David A Stroud

Biomedicines 10: PubMed35203486

2022

Genetic Complementation of ATP Synthase Deficiency Due to Dysfunction of TMEM70 Assembly Factor in Rat.

Applications

Unspecified application

Species

Unspecified reactive species

Aleksandra Marković,Kateřina Tauchmannová,Miroslava Šimáková,Petr Mlejnek,Vilma Kaplanová,Petr Pecina,Alena Pecinová,František Papoušek,František Liška,Jan Šilhavý,Jana Mikešová,Jan Neckář,Josef Houštěk,Michal Pravenec,Tomáš Mráček

Proceedings of the National Academy of Sciences of the United States of America 118: PubMed33879611

2021

Optic atrophy-associated TMEM126A is an assembly factor for the ND4-module of mitochondrial complex I.

Applications

Unspecified application

Species

Unspecified reactive species

Luke E Formosa,Boris Reljic,Alice J Sharpe,Daniella H Hock,Linden Muellner-Wong,David A Stroud,Michael T Ryan

Med (New York, N.Y.) 2:49-73 PubMed33575671

2021

Fatal perinatal mitochondrial cardiac failure caused by recurrent duplications in the locus.

Applications

Unspecified application

Species

Unspecified reactive species

Ann E Frazier,Alison G Compton,Yoshihito Kishita,Daniella H Hock,AnneMarie E Welch,Sumudu S C Amarasekera,Rocio Rius,Luke E Formosa,Atsuko Imai-Okazaki,David Francis,Min Wang,Nicole J Lake,Simone Tregoning,Jafar S Jabbari,Alexis Lucattini,Kazuhiro R Nitta,Akira Ohtake,Kei Murayama,David J Amor,George McGillivray,Flora Y Wong,Marjo S van der Knaap,R Jeroen Vermeulen,Esko J Wiltshire,Janice M Fletcher,Barry Lewis,Gareth Baynam,Carolyn Ellaway,Shanti Balasubramaniam,Kaustuv Bhattacharya,Mary-Louise Freckmann,Susan Arbuckle,Michael Rodriguez,Ryan J Taft,Simon Sadedin,Mark J Cowley,André E Minoche,Sarah E Calvo,Vamsi K Mootha,Michael T Ryan,Yasushi Okazaki,David A Stroud,Cas Simons,John Christodoulou,David R Thorburn

Acta neuropathologica 141:511-526 PubMed33515275

2021

Lipids, lysosomes and mitochondria: insights into Lewy body formation from rare monogenic disorders.

Applications

Unspecified application

Species

Unspecified reactive species

Daniel Erskine,David Koss,Viktor I Korolchuk,Tiago F Outeiro,Johannes Attems,Ian McKeith

Scientific reports 10:15336 PubMed32948797

2020

Decoding mitochondrial heterogeneity in single muscle fibres by imaging mass cytometry.

Applications

Unspecified application

Species

Human

Charlotte Warren,David McDonald,Roderick Capaldi,David Deehan,Robert W Taylor,Andrew Filby,Doug M Turnbull,Conor Lawless,Amy E Vincent

Acta neuropathologica communications 8:103 PubMed32646480

2020

Complex I reductions in the nucleus basalis of Meynert in Lewy body dementia: the role of Lewy bodies.

Applications

Unspecified application

Species

Unspecified reactive species

Christopher Hatton,Amy Reeve,Nichola Zoe Lax,Alasdair Blain,Yi Shiau Ng,Omar El-Agnaf,Johannes Attems,John-Paul Taylor,Doug Turnbull,Daniel Erskine

Neurology. Genetics 6:e464 PubMed32637636

2020

COX deficiency and leukoencephalopathy due to a novel homozygous mutation.

Applications

Unspecified application

Species

Unspecified reactive species

Carola Hedberg-Oldfors,Niklas Darin,Christer Thomsen,Christopher Lindberg,Anders Oldfors

Cell reports 31:107541 PubMed32320651

2020

Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly Complex Factors in the Biogenesis of Complex I.

Applications

Unspecified application

Species

Unspecified reactive species

Luke E Formosa,Linden Muellner-Wong,Boris Reljic,Alice J Sharpe,Thomas D Jackson,Traude H Beilharz,Diana Stojanovski,Michael Lazarou,David A Stroud,Michael T Ryan
View all publications
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