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AB109715

ATP Synthase Immunocapture Kit

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(11 Publications)

250 µg of monoclonal antibodies irreversibly crosslinked to protein G-agarose beads which can immunocapture up to ~125 µg, ~250 µg or ~500 µg respectively of ATP synthase (Complex V) from heart mitochondria.
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Western blot - ATP Synthase Immunocapture Kit (AB109715)
  • WB

Lab

Western blot - ATP Synthase Immunocapture Kit (AB109715)

Using the immunoprecipitation protocol provided, ATP synthase was isolated from various samples by antibody ab109867 crosslinked to protein G-agarose beads (ab109715). Protein bands identities were confirmed by mass spectrometry.

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Key facts

Reacts with

Rat, Cow, Human

Assay type

Quantitative

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Product details

250 μg of monoclonal antibodies irreversibly crosslinked to protein G-agarose beads which can immunocapture up to ~125 μg, ~250 μg or ~500 μg respectively of ATP synthase (Complex V) from heart mitochondria.

ab109715 allows isolation of the ATP synthase complex from small amounts of tissue. This facilitates subsequent analysis of assembly state and activity. Thus the enzyme retains olygomycin sensitive ATP hydrolysis activities after isolation. Finally, the extent of post translational modifications including oxidative damage can be readily analyzed by proteomic approaches or antibody detection of these modifications. Potential uses for ab109715 include but are not limited to examining alterations of ATP synthase subunits in inherited mitochondrial diseases, Alzheimer's disease, angiogenesis, hypertension and aging.

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

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What's included?

{ "values": { "250g": { "sellingSize": "250 µg", "publicAssetCode":"ab109715-250ug", "assetComponentDetails": [ { "size":"2 x 250 µg", "name":"ATP synthase monoclonal antibody coupled agarose beads", "number":"AB109715-CMP01", "productcode":"" } ] } } }
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
+4°C
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Supplementary information

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

ATP synthase also known as Complex V or F1F0-ATPase catalyzes the synthesis of ATP from ADP and inorganic phosphate. The multisubunit enzyme has a mass of approximately 500 kDa and resides in the inner mitochondrial membrane. It also appears in bacterial plasma membranes and the thylakoid membrane of chloroplasts. ATP synthase operates through a rotary mechanism converting a proton gradient into mechanical energy which then converts into chemical energy in the form of ATP.
Biological function summary

ATP synthase functions as a critical component of cellular energy production. As part of the ATP synthase complex it carries out ATP synthesis essential for numerous biological processes. By utilizing a proton-motive force it enables the regeneration of mitochondrial ATP integral for maintaining cellular energy homeostasis. The enzyme's efficient ATP activity highlights its role in ensuring sustained energy supply within cells.

Pathways

ATP synthase plays an important role in the oxidative phosphorylation pathway. This pathway occurs in mitochondria where the enzyme functions alongside other proteins such as NADH dehydrogenase and cytochrome c oxidase. These proteins forming the electron transport chain contribute to establishing the proton gradient required for ATP synthase activity. Additionally ATP synthase activity is closely linked to the citric acid cycle providing the necessary gradient for ATP production.

ATP synthase relates to conditions such as mitochondrial diseases and neurodegenerative disorders. Dysfunctional mitochondrial ATP synthase can lead to energy deficiency and mitochondrial myopathies. It also has connections to proteins like mitochondrial DNA mutations which impact ATP synthase function and cause cellular energy deficits. Furthermore impaired ATP synthase activity can contribute to conditions like Parkinson's disease where energy metabolism disruptions play a role.
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Product protocols

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Target data

See full target information ATP Synthase
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Publications (11)

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

Communications biology 6:836 PubMed37573449

2023

IF1 promotes oligomeric assemblies of sluggish ATP synthase and outlines the heterogeneity of the mitochondrial membrane potential.

Applications

Unspecified application

Species

Unspecified reactive species

Inés Romero-Carramiñana,Pau B Esparza-Moltó,Sonia Domínguez-Zorita,Cristina Nuevo-Tapioles,José M Cuezva

Cell reports 32:108095 PubMed32877677

2020

The Unique Cysteine of F-ATP Synthase OSCP Subunit Participates in Modulation of the Permeability Transition Pore.

Applications

Unspecified application

Species

Unspecified reactive species

Michela Carraro,Kristen Jones,Geppo Sartori,Marco Schiavone,Salvatore Antonucci,Roza Kucharczyk,Jean-Paul di Rago,Cinzia Franchin,Giorgio Arrigoni,Michael Forte,Paolo Bernardi

The Journal of biological chemistry 295:2544-2554 PubMed31974161

2020

Pulse-chase SILAC-based analyses reveal selective oversynthesis and rapid turnover of mitochondrial protein components of respiratory complexes.

Applications

Unspecified application

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Unspecified reactive species

Daniel F Bogenhagen,John D Haley

Nature communications 9:2293 PubMed29895861

2018

α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease.

Applications

Unspecified application

Species

Unspecified reactive species

Marthe H R Ludtmann,Plamena R Angelova,Mathew H Horrocks,Minee L Choi,Margarida Rodrigues,Artyom Y Baev,Alexey V Berezhnov,Zhi Yao,Daniel Little,Blerida Banushi,Afnan Saleh Al-Menhali,Rohan T Ranasinghe,Daniel R Whiten,Ratsuda Yapom,Karamjit Singh Dolt,Michael J Devine,Paul Gissen,Tilo Kunath,Morana Jaganjac,Evgeny V Pavlov,David Klenerman,Andrey Y Abramov,Sonia Gandhi

American journal of physiology. Endocrinology and 311:E449-60 PubMed27406740

2016

Posttranslational modifications and dysfunction of mitochondrial enzymes in human heart failure.

Applications

Unspecified application

Species

Unspecified reactive species

Freya L Sheeran,Salvatore Pepe

Proceedings of the National Academy of Sciences of the United States of America 111:10580-5 PubMed24979777

2014

An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore.

Applications

Unspecified application

Species

Unspecified reactive species

Kambiz N Alavian,Gisela Beutner,Emma Lazrove,Silvio Sacchetti,Han-A Park,Pawel Licznerski,Hongmei Li,Panah Nabili,Kathryn Hockensmith,Morven Graham,George A Porter,Elizabeth A Jonas

International journal of molecular sciences 13:1933-50 PubMed22408432

2012

Glucose-modulated mitochondria adaptation in tumor cells: a focus on ATP synthase and inhibitor Factor 1.

Applications

Unspecified application

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Unspecified reactive species

Rossana Domenis,Elena Bisetto,Davide Rossi,Marina Comelli,Irene Mavelli

Free radical biology & medicine 49:1230-7 PubMed20647045

2010

SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Jianjun Bao,Iain Scott,Zhongping Lu,Liyan Pang,Christopher C Dimond,David Gius,Michael N Sack

Journal of bioenergetics and biomembranes 42:117-23 PubMed20180002

2010

The ectopic F(O)F(1) ATP synthase of rat liver is modulated in acute cholestasis by the inhibitor protein IF1.

Applications

Unspecified application

Species

Unspecified reactive species

Valentina Giorgio,Elena Bisetto,Raffaella Franca,David A Harris,Sabina Passamonti,Giovanna Lippe

The Journal of biological chemistry 284:33982-8 PubMed19801635

2009

Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex.

Applications

Unspecified application

Species

Unspecified reactive species

Valentina Giorgio,Elena Bisetto,Maria Eugenia Soriano,Federica Dabbeni-Sala,Emy Basso,Valeria Petronilli,Michael A Forte,Paolo Bernardi,Giovanna Lippe
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