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ATP5B Protein, Mouse, Recombinant (His & Myc & SUMO)

Catalog No. TMPH-02530
Synonyms: ATP synthase F1 subunit beta, Atp5b, Atp5f1b, ATP synthase subunit beta, mitochondrial

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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
ATP5B Protein, Mouse, Recombinant (His & Myc & SUMO)
Pack Size Availability Price/USD Quantity
20 μg 20 days $ 284.00
100 μg 20 days $ 537.00
1 mg 20 days $ 2,300.00
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Biological Description
Technical Params
Product Properties
Description 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.
Species Mouse
Expression System E. coli
Tag N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged
Accession Number P56480
Synonyms ATP synthase F1 subunit beta, Atp5b, Atp5f1b, ATP synthase subunit beta, mitochondrial
Amino Acid YSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Construction 230-529 aa
Protein Purity > 85% as determined by SDS-PAGE.
Molecular Weight 52.8 kDa (predicted)
Formulation Tris-based buffer,50% glycerol
Reconstitution A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage

Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shipping

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background 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.

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Keywords

ATP5B Protein, Mouse, Recombinant (His & Myc & SUMO) ATP synthase F1 subunit beta Atp5b Atp5f1b ATP synthase subunit beta, mitochondrial recombinant recombinant-proteins proteins protein

 

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