| Product Name | Recombinant Human Prestin (SLC26A5), partial |
|---|---|
| Description | Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses Cytoplasmic domain anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the mbrane in response to changes in the transmbrane voltage. They move towards the Extracellular domain surface following hyperpolarization, and towards the Cytoplasmic domain side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma mbrane. The area decreases when the anion is near the Cytoplasmic domain face of the mbrane (short state), and increases when the ion has crossed the mbrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the mbrane, but does not allow these anions to dissociate and escape to the Extracellular domain space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site . |
| Synonyms | Solute carrier family 26 member 5 |
| Host | Yeast |
| Molecular Weight | 29 |
| Amino Acid Sequence | YRTQSPSYKVLGKLPETDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSNALKRKTGVNPAVIMGARRKAMRKYAKEVGNANMANATVVKADAEVDGEDATKPEEEDGEVKYPPIVIKSTFPEEMQRFMPPGDNVHTVILDFTQVNFIDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTRNRFFENPALWELLFHSIHDAVLGSQLREALAEQEASAPPSQEDLEPNATPATPEA |
| Protein Length | Cytoplasmic Domain, 501-744aa |
| Tag | N-terminal 6xHis-tagged |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Tris-based buffer, 50% glycerol |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| References | Prestin, a cochlear motor protein, is defective in non-syndromic hearing loss.Liu X.Z., Ouyang X.M., Xia X.J., Zheng J., Pandya A., Li F., Du L.L., Welch K.O., Petit C., Smith R.J.H., Webb B.T., Yan D., Arnos K.S., Corey D., Dallos P., Nance W.E., Chen Z.-Y.Hum. Mol. Genet. 12:1155-1162(2003) |
| Background | Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses Cytoplasmic domain anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the mbrane in response to changes in the transmbrane voltage. They move towards the Extracellular domain surface following hyperpolarization, and towards the Cytoplasmic domain side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma mbrane. The area decreases when the anion is near the Cytoplasmic domain face of the mbrane (short state), and increases when the ion has crossed the mbrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the mbrane, but does not allow these anions to dissociate and escape to the Extracellular domain space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site . |
| Supplier | Cusabio |
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