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Human ATP synthase subunit beta (aa 48-529) |
ATPMB Swiss Prot# | | P06576 |
ATPMB Protein names | | ATP synthase subunit beta, mitochondrial (EC 3.6.3.14) |
ATPMB Gene names | | ATP5B (ATPMB) (ATPSB) |
Organism | | Human |
ATPMB Entry name | | ATPB_HUMAN |
ATPMB Codon optimized cDNA(gene) Clone |
ATPMB Cat # | | RPE0258 |
Tag | | ATPMB contains A 6x histidine tag |
ATPMB Formulation | | Liquid |
ATPMB Storage | | Storage at -20℃ to −80℃ Upon receipt. Avoid repeated freeze-thaw cycles. |
ATPMB Applications | | Applications: 1. Codon-optimized cDNA(gene) sequence designed for protein production in both E.coli and Mammalian cell. The cDNA(gene) has been cloned into E.coli expression vector with 6x Histidine tag.2. May be used as RNAi assistance to restore the loss-of-function. |
Recombinant ATPMB Protein |
ATPMB Cat # | | PE0258 |
ATPMB Source | | recombinant |
ATPMB Applications | | Western Blot, SDS-Page or may be used for other applications determined by user |
ATPMB Purity | | >90%, as determined by SDS-PAGE under reducing conditions |
ATPMB Activity | | N/A |
Tag | | ATPMB Contains A 6x histidine tag |
ATPMB Formulation | | Liquid |
ATPMB Storage | | ;. Storage at -20℃ to −80℃ Upon receipt. Avoid repeated freeze-thaw cycles. |
Place Order for Recombinant ATPMB Products | | For pricing and availability Click Here >>> |
ATPMB family | | ATPase alpha/beta chains family |
ATPMB Subcellular locations | | Mitochondrion. Mitochondrion inner membrane. |
ATPMB FUNCTION According to UniProtKB Swiss Prot | | 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. |
ATPMB Sequence | | DDBJ | EMBL | GenBank |
ATPMB 3D structure | | ModBase |
ATPMB interaction | | STRING |
ATPMB Proteomic | | PRIDE |
ATPMB Genome annotation | | Ensembl | GeneID | KEGG | UCSC |
ATPMB Organism specific | | CTD | MGI |
ATPMB Phylogenomics | | eggNOG | GeneTree | HOGENOM | HOVERGEN |
| InParanoid | OrthoDB | PhylomeDB | OMA |
ATPMB Gene expression | | Bgee | ArrayExpress | Genevestigator |
ATPMB Family and domain | | InterPro | PROSITE | ProtoNet |
FOR in vitro RESEARCH USE ONLY |