Recombinant Rat Prestin (Slc26a5), partial

Code CSB-YP866804RA
MSDS
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Source Yeast
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Code CSB-EP866804RA
MSDS
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Source E.coli
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Code CSB-EP866804RA-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP866804RA
MSDS
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Source Baculovirus
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Code CSB-MP866804RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Slc26a5
Uniprot No.
Alternative Names
Slc26a5; PresPrestin; Solute carrier family 26 member 5
Species
Rattus norvegicus (Rat)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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.
Gene References into Functions
  1. work, for the first time, provides proof of concept that the levels of prestin, an otologic serum biomarker, can change after acoustic trauma and hearing loss PMID: 27636386
  2. Prestin expression first appeared at postnatal day 6 (P6) in the auditory brainstem and reached mature level by P14. PMID: 28097024
  3. Molecular dynamics simulations of the STAS domains of rat prestin and human pendrin reveal conformational motions in conserved flexible regions. PMID: 24603188
  4. in chicken STAS, the anion-binding site is lacking because of a local structural rearrangement, indicating that the presence of the STAS anion-binding site is exclusive to mammalian prestin PMID: 26635354
  5. prestin can transport bicarbonate at low rates and acts as an electrogenic transporter for chloride PMID: 22890707
  6. Chronic depolarization decreases prestin expression and possibly contributes to hearing loss and tinnitus. PMID: 21624428
  7. Data suggest that Brn-3c, C/ebpb, and Carf contribute to regulating the expression of prestin. PMID: 21614551
  8. retinoid nuclear transcription factors, GATA-3 and histone acetylation/deacetylation processes may have a regulatory role to play in prestin expression. PMID: 21344672
  9. The results suggest that prestin density, and by implication force production, is similar in low-frequency and high-frequency outer hair cells. PMID: 20525072
  10. Prestin is a member of the SLC26 family of anion transporters that is responsible for outer hair cell electromotility. PMID: 20418376
  11. Although prestin is expressed in vestibular hair cells, it is unlikely that it supports the form of somatic motility observed in outer hair cells. PMID: 14553901
  12. Our data demonstrate that cGMP is significantly more influential than cAMP in modifying the non-linear, voltage-dependent charge displacement in prestin-transfected cells. PMID: 15649974
  13. Significantly up-regulated after noise exposure. Up-regulated gene expression may be in response to injury of proteins, which may be responsible for loss of cochlear amplification. PMID: 17005342
  14. Charge movement by prestin and consequently electromotility depend on the presence of small monovalent anions such as chloride and bicarbonate at the cytoplasmic side of the membrane. PMID: 17120772
  15. From negatively stained prestin particles, the three-dimensional structure was reconstructed at 2 nm resolution assuming 4-fold symmetry, which showed a bullet-shaped particle. PMID: 17998209
  16. data correlate with that of full-length prestin that forms stable tetramers, suggesting that the C-terminal domain play an important role in modulating the properties of the entire prestin. PMID: 18226918
  17. Long-term administration of salicylate enhances prestin expression in rat cochlea. PMID: 19173110

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Subcellular Location
Cell membrane; Multi-pass membrane protein. Note=Lateral wall of outer hair cells.
Protein Families
SLC26A/SulP transporter (TC 2.A.53) family
Tissue Specificity
Specifically expressed in outer hair cells. Not detected in other cells of the organ of Corti.
Database Links
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