ATP synthase subunit beta (ATP5B) Recombinant Protein | ATP5B recombinant protein

Recombinant Mouse ATP synthase subunit beta, mitochondrial (ATP5B), partial

Cat. Num. AAA7110820

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: ATP synthase subunit beta (ATP5B); Recombinant Mouse ATP synthase subunit beta; mitochondrial (ATP5B); partial; ATP5B recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 230-529. Partial
• Sequence: YSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS

• Organism: Mus musculus (Mouse)
• Tag Information: N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged
• Preparation and Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.; Generally, the shelf life of liquid form is 6 months at -20 degree C/-80 degree C.; The shelf life of lyophilized form is 12 months at -20 degree C/-80 degree C.; Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.

SDS-Page

Related Product Information for ATP5B recombinant protein

Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Product Categories/Family for ATP5B recombinant protein

Tags & Cell Markers

References

"A novel principle for conferring selectivity to poly (A)-binding proteins: interdependence of two ATP synthase beta-subunit mRNA-binding proteins." Andersson U., Antonicka H., Houstek J., Cannon B.Biochem. J. 346:33-39 (2000)

NCBI and Uniprot Product Information

• NCBI GI #: 31980648
• NCBI GeneID: 11947
• NCBI Accession #: NP_058054.2
• NCBI GenBank Nucleotide #: NM_016774.3
• UniProt Accession #: P56480; Q0QEP4; Q3TFD7; Q3TIP9; Q3TK44; Q3TWD5; Q3TX28; Q3U6U4; Q3U774; Q3UB69; Q3UF69; Q8CI65
• Molecular Weight: 52.8 kDa
• NCBI Official Full Name: ATP synthase subunit beta, mitochondrial
• NCBI Official Synonym Full Names: ATP synthase, H+ transporting mitochondrial F1 complex, beta subunit
• NCBI Official Symbol: Atp5b
• NCBI Protein Information: ATP synthase subunit beta, mitochondrial
• UniProt Protein Name: ATP synthase subunit beta, mitochondrial
• UniProt Gene Name: Atp5b

Uniprot Description

Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.