Recombinant Human Prestin (SLC26A5) Protein (His/Tag-Free)

Beta LifeScience SKU/CAT #: BLC-08648P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Prestin (SLC26A5) Protein (His/Tag-Free)

Beta LifeScience SKU/CAT #: BLC-08648P
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Product Overview

Description Recombinant Human Prestin (SLC26A5) Protein (His/Tag-Free) is produced by our Yeast expression system. This is a cytoplasmic protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P58743
Target Symbol SLC26A5
Synonyms SLC26A5; PRESPrestin; Solute carrier family 26 member 5
Species Homo sapiens (Human)
Expression System Yeast
Tag N-His/Tag-Free
Protein Length Cytoplasmic Domain
Mol. Weight 29.0kDa
Research Area Neuroscience
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location Cell membrane; Multi-pass membrane protein.
Protein Families SLC26A/SulP transporter (TC 2.A.53) family
Database References

HGNC: 9359

OMIM: 604943

KEGG: hsa:375611

STRING: 9606.ENSP00000304783

UniGene: PMID: 27041369

  • Prestin expression imparts susceptibility to 2-hydroxypropyl-beta-cyclodextrin-induced hearing loss. PMID: 26903308
  • I hypothesize that serum assays of OHC specific protein, prestin, will allow detection and quantification of OHC damage before audiometric testing can identify presence of hearing loss. PMID: 25920562
  • anion-pi interaction is the mechanism for the voltage-dependent response of prestin PMID: 26283790
  • The findings suggest that CASK and the truncated prestin splice isoform contribute to confinement of prestin to the basolateral region of the plasma membrane. PMID: 23542924
  • The effects of fast temperature jumps induced by an infrared (IR) laser in control and prestin (SLC26a5)-transfected human embryonic kidney (HEK) cells, are reproted. PMID: 24138858
  • Calmodulin-prestin interaction may be involved in the medial olivocochlear-mediated modulation of cochlear amplification PMID: 24453323
  • COCH and SLC26A5 mRNA are expressed in specific structures and cells of the inner ear in archival human temporal bone PMID: 23660400
  • prestin subunits are individually functional within a given multimer PMID: 23212912
  • This result implies that in cell membranes prestin oligomerizes to a tetramer. PMID: 21975444
  • Four mutations (C124A, C192A, C260A, and C415A), all in nonconserved cysteinyl residues, significantly differed in their nonlinear capacitance properties compared with wild-type prestin. PMID: 21813750
  • Observational study of genetic testing. (HuGE Navigator) PMID: 20668687
  • These data reveal that the STAS (sulfate transporters and anti-sigma factor antagonist) domain starts immediately after the last transmembrane segment and lies beneath the lipid bilayer. PMID: 20471983
  • Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin PMID: 19926791
  • an essential function of prestin in human auditory processing PMID: 12719379
  • KCNQ4 phosphorylation via PKA and coupling to a complex that may include prestin can lead to the negative activation and the negative resting potential found in adult outer hair cells. PMID: 15660259
  • Because mammals possess differentiated outer hair cells (OHC), they also benefit from a novel electromotile process, powered by the motor protein, prestin. PMID: 16873410
  • Packing of helices and interactions between residues surrounding the sulfate transporter motif is essential for normal prestin activity. PMID: 17151276
  • This is the first genetic and electrophysiological analysis of a human mutation in a coding exon of the pres gene by 47 patients with non-syndromic, sensorineural, mild-to-moderate hearing impairment. PMID: 17786286
  • Cholesterol levels modulate the distribution of prestin within plasma membrane microdomains and affect prestin self-association PMID: 17933870
  • results indicate that an evolutionarily conserved dimeric quaternary structure represents the native and functional state of SLC26 transporters PMID: 18073211
  • Results quantify the relation between membrane cholesterol concentration and prestin-associated charge movement and enhance our understanding of how membrane composition modulates prestin function. PMID: 18567583
  • heterozygosity for the mutation IVS2-2A>G in SLC26A5 gene may not, by itself, be sufficient to cause hearing loss. PMID: 19027966
  • analysis of novel DNA sequence variations in SLC26A5, encoding prestin PMID: 19492055
  • Results are consistent with significant movements in the COOH-terminal domain of prestin upon change in membrane potential, providing the first dynamic information on its molecular rearrangements. PMID: 19515900
  • This indicates that Met-225 in prestin somehow adjusts nonlinear capacitance and the motility of prestin-expressing cells. PMID: 19737539
  • Observational study of gene-disease association. (HuGE Navigator) PMID: 19492055
  • Observational study of gene-disease association. (HuGE Navigator) PMID: 19027966
  • Observational study of gene-disease association. (HuGE Navigator) PMID: 18988928
  • Observational study of genotype prevalence. (HuGE Navigator) PMID: 16086836
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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