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AB235845

Recombinant Human ATP5A protein (Tagged)

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Recombinant Human ATP5A protein (Tagged) is a Human Full Length protein, in the 44 to 553 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

ATP5A, ATP5A1, ATP5AL2, ATPM, ATP5F1A, ATP synthase F1 subunit alpha

3 Images
Mass Spectrometry - Recombinant Human ATP5A protein (Tagged) (AB235845)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human ATP5A protein (Tagged) (AB235845)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab235845 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5A.

Mass Spectrometry - Recombinant Human ATP5A protein (Tagged) (AB235845)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human ATP5A protein (Tagged) (AB235845)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab235845 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5A.

SDS-PAGE - Recombinant Human ATP5A protein (Tagged) (AB235845)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human ATP5A protein (Tagged) (AB235845)

ab235845 analyzed by (Tris-Glycine gel) discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

6x His tag N-Terminus SUMO tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P25705

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

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

Sequence info

[{"sequence":"QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGFEA","proteinLength":"Full Length","predictedMolecularWeight":"71.2 kDa","actualMolecularWeight":null,"aminoAcidEnd":553,"aminoAcidStart":44,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P25705","tags":[{"tag":"6x His","terminus":"N-Terminus"},{"tag":"SUMO","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

ATP5A also known as ATP synthase F1 subunit alpha is a protein important for cellular energy production. As part of the ATP synthase complex it plays a mechanical role in synthesizing ATP from ADP and inorganic phosphate. The ATP5A protein has a molecular weight of approximately 55 kDa and is widely expressed in the inner mitochondrial membrane across different cell types. Its central function lies in its ability to harness the energy of the proton gradient generated by the electron transport chain to catalyze ATP synthesis.
Biological function summary

ATP5A is essential in cellular respiration serving as a catalytic core of the F1 component of ATP synthase. As part of the multi-subunit enzyme complex ATP synthase is responsible for ATP production the primary energy currency in cells. The ATP5A subunit works in conjunction with other subunits of the enzyme oligomer to facilitate the conversion of energy released during oxidative phosphorylation into a usable form. The protein's efficiency in this biological role underpins its importance in sustaining cellular energy homeostasis.

Pathways

ATP5A plays a pivotal role in oxidative phosphorylation and the electron transport chain integral components of cellular respiration. The oxidative phosphorylation pathway depends on this protein to manage the synthesis of ATP molecules while the electron transport chain creates the proton gradient necessary for ATP production. ATP5A is functionally connected to other proteins in these pathways such as ATP5B and cytochrome c oxidase working in a coordinated manner to ensure efficient energy transfer and maintenance.

ATP5A is implicative in mitochondrial disorders and neurodegenerative diseases such as Leigh syndrome and Parkinson's disease. These conditions often arise from deficits in ATP production where ineffective ATP synthase activity can contribute to cellular energy failures. In the context of Parkinson’s disease for instance ATP5A interactions with other proteins like Parkin can contribute to mitochondrial dysfunction an important pathological feature of the disorder. Through such associations alterations in ATP5A activity can significantly impact disease progression and symptomatology.

Specifications

Form

Liquid

General info

Function

Subunit alpha, 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). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed : 37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed : 30146159).

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Post-translational modifications

The N-terminus is blocked.. Acetylated on lysine residues. BLOC1S1 is required for acetylation.

Product protocols

Target data

Subunit alpha, 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). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed : 37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed : 30146159).
See full target information ATP5F1A

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