Analytical Data
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Gene name
SLC26A5
- Application
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Alternative Names
SLC26A5;PRES;Prestin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P58743
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Expression Region
1-447aa
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AA Sequence
MDHAEENEILAATQRYYVERPIFSHPVLQERLHTKDKVPDSIADKLKQAF TCTPKKIRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLA FAMLAAVPPIFGLYSSFYPVIMYCFLGTSRHISIGPFAVISLMIGGVAVR LVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGF VAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAV LQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMG TGISAGFNLKESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVG FSVTISMAKTLANKHGYQVDGNQELIALGLCNSIGSLFQTFSISCSLSRS LVQEGTGGKTQTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQR
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Molecular Weight
81.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SLC26A5, also known as SLC26A5 or Prestin, is a gene that encodes a transmembrane protein critical for the functioning of outer hair cells (OHCs) in the cochlea, playing a significant role in hearing and sound amplification. Research into SLC26A5 has highlighted its importance in the mechanism of electromotility, where OHCs change shape in response to changes in membrane potential, thereby enhancing the sensitivity and selectivity of the auditory system. Understanding the structure and function of the SLC26A5 protein is essential for comprehending various auditory disorders and potential therapeutic interventions. Recombinant SLC26A5 proteins have been developed to study their properties in detail, facilitating investigations into their role in cellular processes and potentially providing insight into the mechanisms underlying hearing loss. These studies are crucial for unveiling the intricacies of cochlear function and may lead to advancements in regenerative medicine and hearing restoration methods.











