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AB96655

Anti-ATP synthase C antibody

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(7 Publications)

Rabbit Polyclonal ATP synthase C antibody. Suitable for WB and reacts with Human samples. Cited in 7 publications. Immunogen corresponding to Synthetic Peptide within Human ATP5MC1.

View Alternative Names

ATP5G1, ATP5MC1, ATP synthase lipid-binding protein, ATP synthase membrane subunit c locus 1, ATP synthase proteolipid P1, ATP synthase proton-transporting mitochondrial F(0) complex subunit C1, ATPase protein 9, ATPase subunit c

1 Images
Western blot - Anti-ATP synthase C antibody (AB96655)
  • WB

Unknown

Western blot - Anti-ATP synthase C antibody (AB96655)

15% SDS PAGE

All lanes:

Western blot - Anti-ATP synthase C antibody (ab96655) at 1/1000 dilution

All lanes:

Molt-4 whole cell lysate at 30 µg

Predicted band size: 14 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human ATP5MC1. The exact immunogen used to generate this antibody is proprietary information.

P05496

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": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/3000", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 40% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

ATP synthase subunit c also known as ATP synthase C ATP-C or ATP synthase C subunit is an integral component of the ATP synthase complex. This protein has a known molecular mass of approximately 8.3 kDa. It is prominently expressed in mitochondrial membranes where it serves as an important part of the proton channel. Its primary function involves facilitating the conversion of proton motive force into rotational mechanical energy which drives ATP synthesis. Through this mechanical action ATP synthase C contributes significantly to energy conversion within cells.
Biological function summary

ATP synthase C functions as a critical component of the ATP synthase enzyme complex also known as FoF1 ATPase or Complex V of the oxidative phosphorylation pathway. This subunit forms a ring structure that allows protons to move across the mitochondrial membrane which is necessary for the synthesis of ATP from ADP and inorganic phosphate. By participating in this synthesis process ATP synthase C impacts cellular energy metabolism affecting various physiological functions dependent on ATP as an energy source.

Pathways

ATP synthase C plays an essential role within the oxidative phosphorylation pathway. This pathway is integral to cellular respiration and is responsible for the majority of ATP production in aerobic organisms. ATP synthase C interacts with other proteins such as the ATP synthase alpha and beta subunits which form the catalytic core of the enzyme. These interactions are central to the energy currency of the cell ensuring efficient energy conversion and transfer.

ATP synthase C is implicated in mitochondrial dysfunctions and associated conditions such as mitochondrial myopathies and neurodegenerative diseases. Mitochondrial myopathies result from defects in the oxidative phosphorylation pathway often involving proteins like cytochrome c oxidase which are important for efficient ATP production. Disorders related to ATP synthase C dysfunction can cause significant impacts on tissues that require high energy reflecting its critical role in maintaining cellular energy balance.

Product protocols

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

Target data

Subunit c, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed : 37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed : 37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). With the subunit a (MT-ATP6), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix (PubMed : 37244256). Protons are taken up via the inlet half-channel and released through the outlet half-channel, following a Grotthuss mechanism (PubMed : 37244256).
See full target information ATP5MC1

Publications (7)

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

International journal of molecular sciences 24: PubMed38069135

2023

Lovastatin Treatment Inducing Apoptosis in Human Pancreatic Cancer Cells by Inhibiting Cholesterol Rafts in Plasma Membrane and Mitochondria.

Applications

Unspecified application

Species

Unspecified reactive species

Momoko Gyoten,Yi Luo,Rina Fujiwara-Tani,Shiori Mori,Ruiko Ogata,Shingo Kishi,Hiroki Kuniyasu

Laboratory investigation; a journal of technical methods and pathology 102:69-79 PubMed34608240

2021

ATP synthase inhibitory factor subunit 1 regulates islet β-cell function via repression of mitochondrial homeostasis.

Applications

Unspecified application

Species

Unspecified reactive species

Kailiang Zhang,Rong Bao,Fengyuan Huang,Kevin Yang,Yishu Ding,Lothar Lauterboeck,Masasuke Yoshida,Qinqiang Long,Qinglin Yang

Redox biology 30:101429 PubMed31981894

2020

Codon optimization is an essential parameter for the efficient allotopic expression of mtDNA genes.

Applications

WB

Species

Human

Caitlin J Lewis,Bhavna Dixit,Elizabeth Batiuk,Carter J Hall,Matthew S O'Connor,Amutha Boominathan

Oncology letters 12:3478-3484 PubMed27900024

2016

Acute effect of lactic acid on tumor-endothelial cell metabolic coupling in the tumor microenvironment.

Applications

WB

Species

Human

Guanqun Zhu,Degui Wang,Shenqian Li,Xuecheng Yang,Yanwei Cao,Yonghua Wang,Haitao Niu

International journal of clinical and experimental 8:12327-36 PubMed26550142

2015

The study of energy metabolism in bladder cancer cells in co-culture conditions using a microfluidic chip.

Applications

Unspecified application

Species

Unspecified reactive species

Xiao-Dong Xu,Shi-Xiu Shao,Yan-Wei Cao,Xue-Cheng Yang,Hao-Qing Shi,You-Lin Wang,Sen-Yao Xue,Xin-Sheng Wang,Hai-Tao Niu

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

WB

Species

Human

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

Cell calcium 56:1-13 PubMed24755650

2014

The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux.

Applications

WB

Species

Human

Elena De Marchi,Massimo Bonora,Carlotta Giorgi,Paolo Pinton
View all publications

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