Specification
| Organism | Bos taurus (Bovine) |
| Expression Host | E.coli |
| Tag Info | N-terminal 10xHis-tagged and C-terminal Myc-tagged |
| Purity | Greater than 85% by SDS-PAGE |
| Uniprot ID | Q28852 |
| Gene Names | ATP5MG |
| Alternative Names | ATP synthase membrane subunit g (ATPase subunit g) (ATP5L) |
| Expression Region | Full Length of Mature Protein(2-103aa ) |
| Molecular Weight | 18.7 kDa |
| Protein Sequence | AEFVRNLAEKAPALVNAAVTYSKPRLATFWYYAKVELVPPTPAEIPTAIQSLKKIINSAKTGSFKQLTVKEALLNGLVATEVWMWFYVGEIIGKRGIIGYDV |
| Form | Liquid or Lyophilization |
| Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. |
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
| Relevance | Mitochondrial membrane ATP synthase 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. Part of the complex F0 domain. Minor subunit located with subunit a in the membrane. |
| Involvement in Disease | |
| Subcellular Location | |
| Protein Families | |
| Tissue Specificity | ATP5MG |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |