Recombinant Human ATPB protein (Tagged) (ab235856)
Key features and details
- Expression system: Escherichia coli
- Purity: > 85% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Human ATPB protein (Tagged) -
Purity
> 85 % SDS-PAGE. -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
YSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGAR ARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAV GYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHL DATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQ DYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMG KLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS -
Predicted molecular weight
53 kDa including tags -
Amino acids
230 to 529 -
Tags
His tag N-Terminus -
Additional sequence information
N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged.
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab235856 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 5B
- ATP synthase H+ transporting mitochondrial F1 complex beta polypeptide
- ATP synthase subunit beta mitochondrial
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. -
Sequence similarities
Belongs to the ATPase alpha/beta chains family. -
Cellular localization
Mitochondrion. 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)
ab235856 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