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AB132441

Recombinant Human ATP6V1A protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human ATP6V1A protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 617 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

ATP6A1, ATP6V1A1, VPP2, ATP6V1A, V-type proton ATPase catalytic subunit A, V-ATPase subunit A, V-ATPase 69 kDa subunit, Vacuolar ATPase isoform VA68, Vacuolar proton pump subunit alpha

1 Images
SDS-PAGE - Recombinant Human ATP6V1A protein (GST tag N-Terminus) (AB132441)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ATP6V1A protein (GST tag N-Terminus) (AB132441)

12.5% SDS-PAGE analysis of ab132441 stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, SDS-PAGE, WB

applications

Biologically active

No

Accession

P38606

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Complementary Products

Primary Antibodies

AB199326

Anti-ATP6V1A antibody [EPR19270]

RabMAb|Recombinant|20ul selling size

Immunocytochemistry/ Immunofluorescence - Anti-ATP6V1A antibody [EPR19270] (AB199326)

  • 4
  • 2
Proteins & Peptides

AB164919

Recombinant Human Zinc finger protein 276 (GST tag N-Terminus)

SDS-PAGE - Recombinant Human Zinc finger protein 276 (GST tag N-Terminus) (AB164919)

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Proteins & Peptides

AB165455

Recombinant Human ZNF358 protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human ZNF358 protein (GST tag N-Terminus) (AB165455)

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  • 0
Proteins & Peptides

AB276192

Recombinant Human Vinculin protein (His tag)

SDS-PAGE - Recombinant Human Vinculin protein (His tag) (AB276192)

  • 0
  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MDFSKLPKILDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED","proteinLength":"Full Length","predictedMolecularWeight":"93.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":617,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P38606","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

ATP6V1A also known as V-ATPase subunit A is a component of the V1 domain of the vacuolar ATPase (V-ATPase) which is a large enzyme responsible for acidifying intracellular compartments. This protein has a mass of approximately 70 kDa and operates in cellular processes by hydrolyzing ATP to drive protons across membranes. ATP6V1A displays significant expression in several cell types including neurons epithelial cells and osteoclasts. The protein enables V-ATPase functionality important for maintaining the pH balance inside cells and organelles facilitating various physiological processes.
Biological function summary

ATP6V1A is an integral part of the V1 domain of the V-ATPase complex a multi-subunit assembly critical for the acidification of intracellular organelles such as lysosomes endosomes and the Golgi apparatus. This activity supports processes like protein degradation receptor-mediated endocytosis and membrane trafficking. The V-ATPase containing ATP6V1A uses energy from ATP hydrolysis to pump protons which is essential for cellular homeostasis and ion transport.

Pathways

ATP6V1A plays an important role in the endocytosis and autophagy pathways. These pathways depend on the acidification of intracellular compartments enabling processes such as the breakdown and recycling of cellular components. ATP6V1A is related to proteins like V-ATPase subunit c (ATP6V1C) and other subunits that form the V-ATPase enzyme. These protein interactions allow the modulation and execution of cellular transport and hormone regulation pathways.

Mutations or dysregulation of ATP6V1A have been linked to renal tubular acidosis and osteoporosis where improper acidification impacts bone resorption and kidney function. The protein connections include its interaction with other V-ATPase subunits like ATP6V0A3 which can also result in osteopetrosis when defective. Such conditions demonstrate how ATP6V1A's role in acidification processes is important for normal physiological function and how its dysfunction leads to disease.
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Specifications

Form

Liquid

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General info

Function

Catalytic subunit of the V1 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 (PubMed : 8463241). 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 (PubMed : 32001091). 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). May play a role in neurite development and synaptic connectivity (PubMed : 29668857).. (Microbial infection) Plays an important role in virion uncoating during Rabies virus replication after membrane fusion. Specifically, participates in the dissociation of incoming viral matrix M proteins uncoating through direct interaction.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Post-translational modifications

Phosphorylation at Ser-384 by AMPK down-regulates its enzyme activity.

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Product protocols

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Target data

Catalytic subunit of the V1 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 (PubMed : 8463241). 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 (PubMed : 32001091). 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). May play a role in neurite development and synaptic connectivity (PubMed : 29668857).. (Microbial infection) Plays an important role in virion uncoating during Rabies virus replication after membrane fusion. Specifically, participates in the dissociation of incoming viral matrix M proteins uncoating through direct interaction.
See full target information ATP6V1A
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Publications (1)

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

Nature chemical biology 15:776-785 PubMed31285595

2019

Covalent targeting of the vacuolar H-ATPase activates autophagy via mTORC1 inhibition.

Applications

Unspecified application

Species

Unspecified reactive species

Clive Yik-Sham Chung,Hijai R Shin,Charles A Berdan,Breanna Ford,Carl C Ward,James A Olzmann,Roberto Zoncu,Daniel K Nomura
View all publications
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