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AB96803

Anti-ATP6V0A2 antibody

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(10 Publications)

Rabbit Polyclonal ATP6V0A2 antibody. Suitable for WB and reacts with Human samples. Cited in 10 publications. Immunogen corresponding to Recombinant Fragment Protein within Human ATP6V0A2 aa 150-450.

View Alternative Names

V-type proton ATPase 116 kDa subunit a 2, V-ATPase 116 kDa subunit a 2, Lysosomal H(+)-transporting ATPase V0 subunit a 2, TJ6, Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2, ATP6V0A2

1 Images
Western blot - Anti-ATP6V0A2 antibody (AB96803)
  • WB

Unknown

Western blot - Anti-ATP6V0A2 antibody (AB96803)

7.5% SDS PAGE

All lanes:

Western blot - Anti-ATP6V0A2 antibody (ab96803) at 1/10000 dilution

Lane 1:

293T whole cell lysate at 30 µg

Lane 2:

A431 whole cell lysate at 30 µg

Lane 3:

H1299 whole cell lysate at 30 µg

Predicted band size: 98 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Human ATP6V0A2 aa 150-450. The exact immunogen used to generate this antibody is proprietary information.

Q9Y487

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>" }, "Mouse": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Rat": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Cow": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 20% 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.

ATP6V0A2 also known as V-ATPase V0 subunit a2 is a component of the vacuolar-type H+-ATPase (V-ATPase) complex. This protein plays a mechanical role in proton translocation across intracellular and plasma membranes. The molecular mass of ATP6V0A2 is approximately 100 kDa. It is widely expressed in many tissues with significant levels in the brain kidney and liver. This expression pattern suggests its functionality is essential across various cellular types and organs.
Biological function summary

ATP6V0A2 contributes to acidification of intracellular compartments such as endosomes lysosomes and the Golgi apparatus. It is part of the larger V-ATPase complex which is critical for processes like protein sorting zymogen activation and receptor-mediated endocytosis. By maintaining the acidic environment within cellular organelles ATP6V0A2 supports the optimal activity of enzymes and influences membrane trafficking impacting cellular homeostasis.

Pathways

ATP6V0A2 influences processes integral to the endocytic and autophagic pathways. These pathways are essential for the degradation and recycling of cellular components. The protein interacts with components of these pathways such as those involved in lysosomal function hinting at its broader involvement in maintaining cellular health. ATP6V0A2 plays a functional role alongside other subunits of the V-ATPase complex in pathways that regulate intracellular pH balance and cellular metabolism.

Defects in ATP6V0A2 are linked to autosomal recessive cutis laxa type II a disorder characterized by loose skin and systemic involvement including developmental delays. Alterations in this protein can also influence the pathology of neurodegenerative diseases. The disorder's connection involves interactions with other proteins such as collagens which are affected by changes in the pH of the secretory pathway highlighting the importance of ATP6V0A2 in maintaining proper cellular microenvironments.

Product protocols

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

Target data

Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery (PubMed : 16415858). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (PubMed : 18157129). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed : 28296633).
See full target information ATP6V0A2

Publications (10)

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

Nature structural & molecular biology 32:2076-2087 PubMed40646309

2025

A heterotrimeric protein complex assembles the metazoan V-ATPase upon dissipation of proton gradients.

Applications

Unspecified application

Species

Unspecified reactive species

Christopher Nardone,Julian Mintseris,Dingwei He,Justine C Rutter,Benjamin L Ebert,Steven P Gygi,Tom Rapoport

Cellular and molecular life sciences : CMLS 82:4 PubMed39680136

2024

Golgi pH elevation due to loss of V-ATPase subunit V0a2 function correlates with tissue-specific glycosylation changes and globozoospermia.

Applications

Unspecified application

Species

Unspecified reactive species

Johannes Kopp,Denise Jahn,Guido Vogt,Anthi Psoma,Edoardo Ratto,Willy Morelle,Nina Stelzer,Ingrid Hausser,Anne Hoffmann,Miguel Rodriguez de Los Santos,Leonard A Koch,Björn Fischer-Zirnsak,Christian Thiel,Wilhelm Palm,David Meierhofer,Geert van den Bogaart,François Foulquier,Andreas Meinhardt,Uwe Kornak

Cell death discovery 10:337 PubMed39048556

2024

Epirubicin induces cardiotoxicity through disrupting ATP6V0A2-dependent lysosomal acidification and triggering ferroptosis in cardiomyocytes.

Applications

Unspecified application

Species

Unspecified reactive species

Mingming Zhang,Xin Wu,Yuting Wen,Zhiquan Li,Fuzhong Chen,Yu Zou,Xiaoyu Dong,Xinjian Liu,Junhong Wang

International journal of molecular sciences 25: PubMed38396846

2024

The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa.

Applications

Unspecified application

Species

Unspecified reactive species

Anh Chu,Yeqi Yao,Miroslawa Glibowicka,Charles M Deber,Morris F Manolson

The EMBO journal 42:e113105 PubMed37409525

2023

TECPR1 is activated by damage-induced sphingomyelin exposure to mediate noncanonical autophagy.

Applications

Unspecified application

Species

Unspecified reactive species

Namrita Kaur,Laura Rodriguez de la Ballina,Håvard Styrkestad Haukaas,Maria Lyngaas Torgersen,Maja Radulovic,Michael J Munson,Alan Sabirsh,Harald Stenmark,Anne Simonsen,Sven R Carlsson,Alf Håkon Lystad

American journal of physiology. Cell physiology 318:C1166-C1177 PubMed32320289

2020

A common genetic variant in zinc transporter ZnT2 (Thr288Ser) is present in women with low milk volume and alters lysosome function and cell energetics.

Applications

Unspecified application

Species

Unspecified reactive species

Olivia C Rivera,Donna T Geddes,Shiran Barber-Zucker,Raz Zarivach,Annie Gagnon,David I Soybel,Shannon L Kelleher

Journal of immunology (Baltimore, Md. : 1950) 204:2818-2828 PubMed32269094

2020

Role of V-ATPase a3-Subunit in Mouse CTL Function.

Applications

Unspecified application

Species

Unspecified reactive species

Praneeth Chitirala,Keerthana Ravichandran,Claudia Schirra,Hsin-Fang Chang,Elmar Krause,Uli Kazmaier,Marcel A Lauterbach,Jens Rettig

Autophagy 13:670-685 PubMed28129027

2017

Disruption of the vacuolar-type H-ATPase complex in liver causes MTORC1-independent accumulation of autophagic vacuoles and lysosomes.

Applications

Unspecified application

Species

Unspecified reactive species

Sandra Kissing,Sönke Rudnik,Markus Damme,Renate Lüllmann-Rauch,Atsuhiro Ichihara,Uwe Kornak,Eeva-Liisa Eskelinen,Sabrina Jabs,Jörg Heeren,Jef K De Brabander,Albert Haas,Paul Saftig

Cell death & disease 7:e2513 PubMed27929536

2016

Hyperhomocysteinemia causes ER stress and impaired autophagy that is reversed by Vitamin B supplementation.

Applications

Unspecified application

Species

Unspecified reactive species

Madhulika Tripathi,Cheng Wu Zhang,Brijesh Kumar Singh,Rohit Anthony Sinha,Kyaw Thu Moe,Deidre Anne DeSilva,Paul Michael Yen

The Journal of biological chemistry 290:14166-80 PubMed25903133

2015

Vacuolar ATPase in phagosome-lysosome fusion.

Applications

Unspecified application

Species

Unspecified reactive species

Sandra Kissing,Christina Hermsen,Urska Repnik,Cecilie Kåsi Nesset,Kristine von Bargen,Gareth Griffiths,Atsuhiro Ichihara,Beth S Lee,Michael Schwake,Jef De Brabander,Albert Haas,Paul Saftig
View all publications

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