Prestin (SLC26A5) Recombinant Protein | SLC26A5 recombinant protein

Recombinant Human Prestin (SLC26A5), partial

Cat. Num. AAA956246

• Gene Names: SLC26A5; PRES; DFNB61
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Prestin (SLC26A5); Recombinant Human Prestin (SLC26A5); partial; Solute carrier family 26 member 5; SLC26A5 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 501-744. Partial
• Sequence: YRTQSPSYKVLGKLPETDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSNALKRKTGVNPAVIMGARRKAMRKYAKEVGNANMANATVVKADAEVDGEDATKPEEEDGEVKYPPIVIKSTFPEEMQRFMPPGDNVHTVILDFTQVNFIDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTRNRFFENPALWELLFHSIHDAVLGSQLREALAEQEASAPPSQEDLEPNATPATPEA

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for SLC26A5 recombinant protein

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.

Product Categories/Family for SLC26A5 recombinant protein

Neuroscience

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) Sequence of an alternatively spliced isoform of prestin (SLC26A5e) .Mount D.B.The DNA sequence of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003)

NCBI and Uniprot Product Information

• NCBI GI #: 269784651
• NCBI GeneID: 375611
• NCBI Accession #: NP_001161434.1
• NCBI GenBank Nucleotide #: NM_001167962.1
• UniProt Accession #: P58743; Q496J2; Q7Z7F3; Q86UF8; Q86UF9; Q86UG0
• Molecular Weight: 29 kDa
• NCBI Official Full Name: prestin isoform e
• NCBI Official Synonym Full Names: solute carrier family 26 (anion exchanger), member 5
• NCBI Official Symbol: SLC26A5
• NCBI Official Synonym Symbols: PRES; DFNB61
• NCBI Protein Information: prestin
• UniProt Protein Name: Prestin
• Protein Family: Prestin
• UniProt Gene Name: SLC26A5
• UniProt Synonym Gene Names: PRES
• UniProt Entry Name: S26A5_HUMAN

NCBI Description

This gene encodes a member of the SLC26A/SulP transporter family. The protein functions as a molecular motor in motile outer hair cells (OHCs) of the cochlea, inducing changes in cell length that act to amplify sound levels. The transmembrane protein is an incomplete anion transporter, and does not allow anions to cross the cell membrane but instead undergoes a conformational change in response to changes in intracellular Cl- levels that results in a change in cell length. The protein functions at microsecond rates, which is several orders of magnitude faster than conventional molecular motor proteins. Mutations in this gene are potential candidates for causing neurosensory deafness. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Nov 2009]

Uniprot Description

SLC26A5: 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. Defects in SLC26A5 are the cause of deafness autosomal recessive type 61 (DFNB61). A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. 5 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; Membrane protein, multi-pass; Transporter; Transporter, SLC family

Chromosomal Location of Human Ortholog: 7q22.1

Cellular Component: basolateral plasma membrane; cytoplasm; integral to plasma membrane; lateral plasma membrane

Molecular Function: anion:anion antiporter activity; bicarbonate transmembrane transporter activity; chloride channel activity; oxalate transmembrane transporter activity; protein homodimerization activity; secondary active sulfate transmembrane transporter activity; spectrin binding; sulfate transmembrane transporter activity; transcription factor binding

Biological Process: bicarbonate transport; fructose transport; oxalate transport; positive regulation of cell size; protein tetramerization; regulation of cell shape; regulation of intracellular pH; regulation of membrane potential; response to drug; response to salicylic acid stimulus; sensory perception of sound