Analytical Data
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Gene name
SLC26A5
- Application
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Alternative Names
Solute carrier family 26 member 5
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Species
Human
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Source
Yeast
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Tag
N- His
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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
501-744aa
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Molecular Weight
29 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
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Protein Description
SLC26A5, also known as Prestin, is a vital membrane protein predominantly expressed in the outer hair cells of the cochlea in the inner ear, playing a crucial role in mammalian hearing. This protein functions as an electromechanical transducer, enabling the amplification of sound vibrations through its unique properties of electromotility. Understanding SLC26A5 is essential not only for unraveling the mechanisms of auditory function but also for exploring potential therapeutic strategies for hearing impairments. The study of recombinant SLC26A5 protein has gained significance as experimental approaches aim to elucidate the structure-function relationship of this protein, as well as its interactions with other cellular components. By utilizing recombinant DNA technology, researchers can produce SLC26A5 in vitro, enabling detailed biophysical and biochemical analyses. Advances in techniques such as cryo-electron microscopy and mutagenesis have further accelerated the exploration of this protein's conformational dynamics and its role in the cochlear amplification process. Investigating the recombinant SLC26A5 offers insights into not only fundamental auditory biology but also the potential development of innovative treatments for auditory dysfunctions, thereby bridging basic research and clinical applications in audiology.
