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

Catalog No. TMPH-02530 Copy Product Info

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.

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

Catalog No. TMPH-02530

Copy Product Info

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

Pack Size	Price	USA Stock	Global Stock
5 μg	$105	20 days	20 days
10 μg	$169	20 days	20 days
20 μg	$283	20 days	20 days
50 μg	$428	20 days	20 days
100 μg	$590	20 days	20 days
200 μg	$913	20 days	20 days
500 μg	$1,620	20 days	20 days
1 mg	$2,530	20 days	20 days

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In stock · Estimated delivery: USA Stock (1-2 days) Global Stock (5-7 days)

For research use only—not for human use. No sales to individuals. Use as intended only.

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Biological Activity	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
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-10xHis-SUMO, C-Myc
Accession Number	P56480
Synonyms	mitochondrial,Atp5f1b,Atp5b,ATP synthase subunit beta, mitochondrial,ATP synthase F1 subunit beta
Amino Acid	YSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS
Construction	230-529 aa
Protein Purity	> 85% as determined by SDS-PAGE.
Molecular Weight	52.8 kDa (predicted)
Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Tris-based buffer, 50% glycerol
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, lyophilized powders are shipped with blue ice, while solutions are shipped with dry ice.
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

ATP synthase subunit β, mitochondrial ATP synthase subunit b, mitochondrial ATP synthase F1 subunit β ATP synthase F1 subunit b