AB109801

Complex IV Immunocapture Kit

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(11 Publications)

ab109801 Complex IV Immunocapture Kit allows isolation of the cytochrome c oxidase complex from small amounts of tissue.

別名を表示する

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

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Supplier Data

Immunoprecipitation - Complex IV Immunocapture Kit (AB109801)

Complex IV immunoprecipitation using antibody ab109863/MS101c crosslinked to protein G-agarose beads as product ab109801

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Key facts

交差種

Cow, Human

アッセイタイプ

Quantitative

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製品の詳細

ab109801 Complex IV Immunocapture Kit allows isolation of the cytochrome c oxidase complex from small amounts of tissue.

250 μg, 500 μg or 750 μg monoclonal antibodies irreversibly crosslinked to protein G-agarose beads which can immunocapture ~25 μg, ~50 μg or ~75 μg respectively of Complex IV from heart mitochondria.

This kit facilitates subsequent analysis of both assembly state and accrued post-translational modifications of all 13 subunits of Complex IV. The immunoprecipitated Complex IV shows cytochrome c oxidase activity while bound to the beads and this activity is fully sensitive to cyanide. Uses for ab109801 include but are not limited to examining alterations of Complex IV subunits in inherited mitochondrial diseases, Alzheimer's disease, schizophrenia and cancer.

Note: The immunocapture protocol for this kit requires Abcam detergent lauryl maltoside (ab109857/MS910).

**Related products**Review the , or the full to learn about more assays for metabolites, metabolic enzymes, mitochondrial function, and oxidative stress, and also how to assay metabolic function in live cells using your plate reader.

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製品内容

{ "values": { "250g": { "sellingSize": "250 µg", "publicAssetCode":"ab109801-250ug", "assetComponentDetails": [ { "size":"1 x 250 µg", "name":"Monoclonal Complex IV antibody irreversibly crosslinked to protein G-agarose beads", "number":"AB109801-CMP01", "productcode":"" } ] } } }

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出荷温度及び保存条件

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

+4°C

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補足情報

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

Complex IV also known as cytochrome c oxidase is an important component of the electron transport chain in mitochondria. This enzyme complex has significant mass approximately 204 kDa and operates primarily in the inner mitochondrial membrane. It catalyzes the transfer of electrons from cytochrome c to oxygen facilitating ATP generation. Complex IV is ubiquitously expressed in all tissues with higher expression in organs with high energy demands like heart and skeletal muscle. This enzyme is composed of multiple subunits encoded by both mitochondrial and nuclear DNA.

Biological function summary

Cytochrome c oxidase plays a critical role in cellular respiration. It forms part of the larger enzyme complex which also includes Complex I II and III. These complexes work together to create a proton gradient across the inner mitochondrial membrane essential for ATP synthesis via oxidative phosphorylation. This enzyme's activity is measured through assays like the cytochrome c oxidase assay which evaluates its function in various tissues. These assays help researchers understand how effectively electrons are being transferred and protons are driven across the membrane.

Pathways

Complex IV is integral to the oxidative phosphorylation pathway and the broader mitochondrial respiratory chain. It interacts closely with cytochrome c a small heme protein that shuttles electrons between Complex III (cytochrome c reductase) and Complex IV. Through these interactions the proton gradient is established enabling ATP synthase to convert chemical energy into usable cell energy. This process significantly impacts cellular metabolism and energy production influencing how efficiently cells function.

Complex IV dysfunction is associated with mitochondrial diseases and certain neurodegenerative disorders. For instance defects in cytochrome c oxidase lead to conditions like Leigh syndrome a severe neurological disorder. Also studies show that disruptions in the electron transport chain involving Complex IV relate closely to Alzheimer’s disease. Alterations in proteins like cytochrome c which work in tandem with Complex IV can exacerbate these conditions highlighting the importance of this target in understanding and potentially treating these diseases.

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製品プロトコール

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

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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 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

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文献 (11)

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

Redox biology 37:101725 PubMed32971361

2020

Glutathionylated and Fe-S cluster containing hMIA40 (CHCHD4) regulates ROS and mitochondrial complex III and IV activities of the electron transport chain.

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Venkata Ramana Thiriveedi,Ushodaya Mattam,Prasad Pattabhi,Vandana Bisoyi,Noble Kumar Talari,Thanuja Krishnamoorthy,Naresh Babu V Sepuri

American journal of physiology. Cell physiology 316:C862-C875 PubMed30865517

2019

Acute increases in -GlcNAc indirectly impair mitochondrial bioenergetics through dysregulation of LonP1-mediated mitochondrial protein complex turnover.

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JaLessa N Wright,Gloria A Benavides,Michelle S Johnson,Willayat Wani,Xiaosen Ouyang,Luyun Zou,Helen E Collins,Jianhua Zhang,Victor Darley-Usmar,John C Chatham

Nature 554:128-132 PubMed29364879

2018

Mitochondrial translation requires folate-dependent tRNA methylation.

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Raphael J Morscher,Gregory S Ducker,Sophia Hsin-Jung Li,Johannes A Mayer,Zemer Gitai,Wolfgang Sperl,Joshua D Rabinowitz

The Journal of biological chemistry 291:24188-24199 PubMed27679486

2016

Identification of Small Molecule Inhibitors of Human Cytochrome c Oxidase That Target Chemoresistant Glioma Cells.

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Claudia R Oliva,Tahireh Markert,Larry J Ross,E Lucile White,Lynn Rasmussen,Wei Zhang,Maaike Everts,Douglas R Moellering,Shannon M Bailey,Mark J Suto,Corinne E Griguer

Molecular and cellular biology 35:1139-56 PubMed25605331

2015

C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization.

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Marjorie Desmurs,Michelangelo Foti,Etienne Raemy,Frédéric Maxime Vaz,Jean-Claude Martinou,Amos Bairoch,Lydie Lane

Journal of medical genetics 49:10-5 PubMed22114105

2011

Defective NDUFA9 as a novel cause of neonatally fatal complex I disease.

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B J C van den Bosch,M Gerards,W Sluiter,A P A Stegmann,E L C Jongen,D M E I Hellebrekers,R Oegema,E H Lambrichs,H Prokisch,K Danhauser,K Schoonderwoerd,I F M de Coo,H J M Smeets

Cell metabolism 14:428-34 PubMed21907147

2011

Mutations in MTFMT underlie a human disorder of formylation causing impaired mitochondrial translation.

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Elena J Tucker,Steven G Hershman,Caroline Köhrer,Casey A Belcher-Timme,Jinal Patel,Olga A Goldberger,John Christodoulou,Jonathon M Silberstein,Matthew McKenzie,Michael T Ryan,Alison G Compton,Jacob D Jaffe,Steven A Carr,Sarah E Calvo,Uttam L RajBhandary,David R Thorburn,Vamsi K Mootha

American journal of physiology. Cell physiology 296:C1218-26 PubMed19295170

2009

Loss of function of Sco1 and its interaction with cytochrome c oxidase.

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Lukas Stiburek,Katerina Vesela,Hana Hansikova,Helena Hulkova,Jiri Zeman

Human molecular genetics 16:2472-81 PubMed17656376

2007

The A3243G tRNALeu(UUR) mutation induces mitochondrial dysfunction and variable disease expression without dominant negative acting translational defects in complex IV subunits at UUR codons.

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George M C Janssen,Paul J Hensbergen,Frans J van Bussel,Crina I A Balog,J Antonie Maassen,André M Deelder,Anton K Raap

Biotechnology and applied biochemistry 48:167-78 PubMed17508937

2007

Small-scale immunopurification of cytochrome c oxidase for a high-throughput multiplexing analysis of enzyme activity and amount.

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James Murray,Birgit Schilling,Richard H Row,Chris B Yoo,Bradford W Gibson,Michael F Marusich,Roderick A Capaldi

View all publications

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Complex IV Immunocapture Kit