Recombinant Human ATP5A protein (His tag) (ab235862)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Human ATP5A protein (His tag)
See all ATP5A proteins and peptides -
Purity
> 90 % SDS-PAGE. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAE EMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVG EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGI KAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLY CIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSG CSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQI FLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREV AAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR GYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEI VTNFLAGFEA -
Predicted molecular weight
59 kDa including tags -
Amino acids
44 to 553 -
Tags
His tag N-Terminus -
Additional sequence information
N-terminal 6xHis-tagged. Full length mature chain without transit peptide.
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab235862 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 7.2
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
General Info
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Alternative names
- ATP synthase alpha chain
- ATP synthase alpha chain, mitochondrial
- ATP synthase subunit alpha
see all -
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites. -
Tissue specificity
Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. -
Sequence similarities
Belongs to the ATPase alpha/beta chains family. -
Post-translational
modificationsThe N-terminus is blocked. -
Cellular localization
Mitochondrion inner membrane. Peripheral membrane protein. - Information by UniProt
Images
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (1)
ab235862 has been referenced in 1 publication.
- Zhao Q et al. Targeting Mitochondria-Located circRNA SCAR Alleviates NASH via Reducing mROS Output. Cell 183:76-93.e22 (2020). PubMed: 32931733