Recombinant Human ATP synthase subunit beta, mitochondrial (ATP5B), partial
| Product Name | Recombinant Human ATP synthase subunit beta, mitochondrial (ATP5B), partial |
|---|---|
| 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. |
| Synonyms | ATPMB, ATPSB |
| Host | E.coli |
| Molecular Weight | 52.8 kDa |
| Amino Acid Sequence | YSVFAGVGERTREGNDLYHEMIESGVINL kdaTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS |
| Protein Length | Partial, 230-529aa |
| Tag | N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Tris-based buffer, 50% glycerol |
| Purity | Greater than 85% as determined by SDS-PAGE. |
| References |
"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) |
| Background | 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. |
| Supplier | Cusabio |
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