癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
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Slc26a5 Rabbit pAb
Slc26a5 Rabbit pAb
- 产品详情
- 实验流程
- 背景知识
Application 
| IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | P58743 |
| Predicted | Rat, Pig, Human, Mouse, Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 81264 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human Slc26a5 |
| Epitope Specificity | 201-300/744 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | Preservative: 0.02% Proclin300, Constituents: 1% BSA, 0.01M PBS, pH7.4. |
| SUBCELLULAR LOCATION | Cell membrane; Multi-pass membrane protein. Note=Lateral wall of outer hair cells. |
| DISEASE | Deafness, autosomal recessive, 61 (DFNB61) [MIM:613865]: 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. Note=The disease is caused by mutations affecting the gene represented in this entry. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | 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] |
| Gene ID | 375611 |
|---|---|
| Other Names | Prestin, Solute carrier family 26 member 5, SLC26A5 (HGNC:9359), PRES |
| Dilution | IHC-P=1:100-500,IHC-F=1:100-500,ICC/IF=1:100-500,IF=1:100-500 |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | SLC26A5 (HGNC:9359) |
|---|---|
| Synonyms | PRES |
| Function | Voltage-sensitive motor protein that drives outer hair cell (OHC) electromotility (eM) and participates in sound amplification in the hearing organ (By similarity). Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement of a charged voltage sensor across the lipid membrane (By similarity). The nature of the voltage sensor is not completely clear, and two models compete. In the first model, acts as an incomplete transporter where intracellular chloride anion acts as extrinsic voltage sensor that drives conformational change in the protein which is sufficient to produce a length change in the plane of the membrane and hence in the length of the OHC (By similarity). The second model in which multiple charged amino acid residues are distributed at the intracellular and extracellular membrane interfaces that form an intrinsic voltage sensor, whose movement produces the non-linear capacitance (NLC) (PubMed:34390643). However, the effective voltage sensor may be the result of a hybrid voltage sensor, assembled from intrinsic charge (charged residues) and extrinsic charge (bound anion) (By similarity). Notably, binding of anions to the anion-binding pocket partially neutralizes the intrinsic positive charge rather than to form an electrically negative sensor, therefore remaining charge may serve as voltage sensor that, after depolarization, moves from down (expanded state) to up (contracted) conformation, which is accompanied by an eccentric contraction of the intermembrane cross-sectional area of the protein as well as a major increase in the hydrophobic thickness of the protein having as consequences the plasma membrane thickening and the cell contraction after membrane depolarization (PubMed:34390643). The anion-binding pocket transits from the inward-open (Down) state, where it is exposed toward the intracellular solvent in the absence of anion, to the occluded (Up) state upon anion binding (PubMed:34390643). Salicylate competes for the anion-binding site and inhibits the voltage-sensor movement, and therefore inhibits the charge transfer and electromotility by displacing Cl(-) from the anion-binding site and by preventing the structural transitions to the contracted state (PubMed:34390643). In addition, can act as a weak Cl(-)/HCO3(-) antiporter across the cell membrane and so regulate the intracellular pH of the outer hair cells (OHCs), while firstly found as being unable to mediate electrogenic anion transport (By similarity). Moreover, supports a role in cardiac mechanical amplification serving as an elastic element to enhance the actomyosin- based sarcomere contraction system (By similarity). |
| Cellular Location | Lateral cell membrane; Multi-pass membrane protein. Note=Localized at the lateral cell membrane of outer hair cells (By similarity). Alters profoundly the shape of its surrounding lipid bilayer (PubMed:34390643). {ECO:0000250, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34390643} |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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