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AB176609

Anti-ATP6AP1/ATP6S1 antibody

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(3 Publications)

Rabbit Polyclonal ATP6AP1/ATP6S1 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human ATP6AP1 aa 1-250.

View Alternative Names

ATP6IP1, ATP6S1, VATPS1, XAP3, ATP6AP1, V-type proton ATPase subunit S1, V-ATPase subunit S1, Protein XAP-3, V-ATPase Ac45 subunit, V-ATPase S1 accessory protein, Vacuolar proton pump subunit S1

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ATP6AP1/ATP6S1 antibody (AB176609)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ATP6AP1/ATP6S1 antibody (AB176609)

Immunohistochemical staining of formalin-fixed paraffin-embedded Human brain tissue labeling ATP6AP1/ATP6S1 with ab176609 at 1/100 dilution showing membrane staining.

Western blot - Anti-ATP6AP1/ATP6S1 antibody (AB176609)
  • WB

Supplier Data

Western blot - Anti-ATP6AP1/ATP6S1 antibody (AB176609)

All lanes:

Western blot - Anti-ATP6AP1/ATP6S1 antibody (ab176609) at 1/500 dilution

All lanes:

Fetal kidney lysate

Predicted band size: 52 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human ATP6AP1 aa 1-250. The exact immunogen used to generate this antibody is proprietary information.

Q15904

Reactivity data

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Properties and storage information

Form
Lyophilized
Reconstitution
reconstitute with water at 200µL
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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.

ATP6AP1 also known as ATPase H+ Transporting Accessory Protein 1 is a component of the V-ATPase complex. This protein weighing about 55 kDa assists in the acidification of organelles such as endosomes and lysosomes. ATP6AP1 exists mainly in the endoplasmic reticulum and is also found in the Golgi apparatus. It interacts with other proteins to maintain proper pH levels in intracellular compartments which is important for various cellular processes.
Biological function summary

ATP6AP1 acts as a regulatory subunit of the vacuolar ATPase (V-ATPase) proton pump complex. This complex is responsible for pumping protons across intracellular and plasma membranes which acidifies vacuoles and lysosomal compartments. Such acidification is necessary for degradation processes within lysosomes. Its association with V-ATPase shows that ATP6AP1 influences pH balance rather than enzyme activity playing a role in cellular homeostasis and trafficking.

Pathways

ATP6AP1 functions within both the acidification and autophagy pathways. Maintaining the acidic environment needed for endocytic and autophagic pathways ensures proper degradation and recycling of cellular components. ATP6AP1 associates with proteins like ATP6V1A an important component of the V-ATPase linking it to proton translocation processes. The protein’s activity within these pathways supports vesicle acidification needed for processes like protein degradation and cellular waste elimination.

ATP6AP1 mutations have connections to glycosylation disorders and congenital disorders of glycosylation type IIH. Alterations in the gene encoding ATP6AP1 can lead to improper protein glycosylation and trafficking within the cell. This malfunction is associated with symptoms that affect multiple systems and cause developmental issues. Additionally ATP6AP1 has an established relationship with another protein ATP6V0A2 through pathways linked to glycosylation demonstrating its importance in maintaining cellular function and health.

Product protocols

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

Target data

Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (PubMed : 33065002). Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity (PubMed : 27231034). Involved in membrane trafficking and Ca(2+)-dependent membrane fusion (PubMed : 27231034). May play a role in the assembly of the V-type ATPase complex (Probable). 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). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (By similarity).
See full target information ATP6AP1

Publications (3)

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

Nature 603:159-165 PubMed35197629

2022

Low-dose metformin targets the lysosomal AMPK pathway through PEN2.

Applications

Unspecified application

Species

Unspecified reactive species

Teng Ma,Xiao Tian,Baoding Zhang,Mengqi Li,Yu Wang,Chunyan Yang,Jianfeng Wu,Xiaoyan Wei,Qi Qu,Yaxin Yu,Shating Long,Jin-Wei Feng,Chun Li,Cixiong Zhang,Changchuan Xie,Yaying Wu,Zheni Xu,Junjie Chen,Yong Yu,Xi Huang,Ying He,Luming Yao,Lei Zhang,Mingxia Zhu,Wen Wang,Zhi-Chao Wang,Mingliang Zhang,Yuqian Bao,Weiping Jia,Shu-Yong Lin,Zhiyun Ye,Hai-Long Piao,Xianming Deng,Chen-Song Zhang,Sheng-Cai Lin

Cell death and differentiation 29:1240-1254 PubMed34997207

2022

SARS-CoV-2 non-structural protein 6 triggers NLRP3-dependent pyroptosis by targeting ATP6AP1.

Applications

Unspecified application

Species

Unspecified reactive species

Xiao Sun,Yingzhi Liu,Ziheng Huang,Wenye Xu,Wei Hu,Lina Yi,Zhe Liu,Hung Chan,Judeng Zeng,Xiaodong Liu,Huarong Chen,Jun Yu,Francis Ka Leung Chan,Siew Chien Ng,Sunny Hei Wong,Maggie Haitian Wang,Tony Gin,Gavin Matthew Joynt,David Shu Cheong Hui,Xuan Zou,Yuelong Shu,Christopher Hon Ki Cheng,Shisong Fang,Huanle Luo,Jing Lu,Matthew Tak Vai Chan,Lin Zhang,William Ka Kei Wu

The Journal of experimental medicine 214:3707-3729 PubMed29127204

2017

Mutations in the X-linked cause a glycosylation disorder with autophagic defects.

Applications

Unspecified application

Species

Unspecified reactive species

Maria A Rujano,Magda Cannata Serio,Ganna Panasyuk,Romain Péanne,Janine Reunert,Daisy Rymen,Virginie Hauser,Julien H Park,Peter Freisinger,Erika Souche,Maria Clara Guida,Esther M Maier,Yoshinao Wada,Stefanie Jäger,Nevan J Krogan,Oliver Kretz,Susana Nobre,Paula Garcia,Dulce Quelhas,Thomas D Bird,Wendy H Raskind,Michael Schwake,Sandrine Duvet,Francois Foulquier,Gert Matthijs,Thorsten Marquardt,Matias Simons
View all publications

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