|Other Accession||NP_109652.3, 375611, 80979 (mouse), 83891 (rat)|
|Predicted||Human, Mouse, Rat, Pig, Dog, Cow|
|Calculated MW||81264 Da|
|Other Names||Prestin, Solute carrier family 26 member 5, SLC26A5, PRES|
|Format||0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Prestin (aa399-411) Antibody (internal region) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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 anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic 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 membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity).|
|Cellular Location||Cell membrane; Multi-pass membrane protein. Note=Lateral wall of outer hair cells.|
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Provided below are standard protocols that you may find useful for product applications.
The immunizing peptide represents part of an extracellular loop.
Structure of the cytosolic portion of the motor protein prestin and functional
role of the STAS domain in SLC26/SulP anion transporters. Pasqualetto E, Aiello R, Gesiot L, Bonetto G, Bellanda M, Battistutta R. J Mol Biol. 2010 Jul 16;400(3):448-62. PMID: 20471983
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