Recombinant Human ATP synthase subunit beta, mitochondrial(ATP5B)

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Product Code: CSB-YP002350HU
Size: 10μg/50μg/100μg/200μg/500μg/1mg
Species of origin: Homo sapiens (Human)
Application: SDS-PAGE
Express system: Yeast
More Information
Uniprot NO. P06576
Target/Protein ATP5B
Species of origin Homo sapiens (Human)
Biologically Active Not Test
Nature Recombinant
Protein description Full?length?of?mature?protein?
MW of Fusion Proten 53.8 kDa
Expression Region 48-529aa
Expression System Yeast
Purity Greater than 90% as determined by SDS-PAGE.
Application SDS-PAGE
Tag info N-terminal 6xHis-tagged
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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reference "The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression." Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S., Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C. Genomics 5:829-843(1989)
Relevance 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.
Research areas Tags & Cell Markers

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