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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TECTB Rabbit pAb
TECTB Rabbit pAb
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | Q96PL2 |
| Reactivity | Pig, Human, Rabbit, Dog |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 36956 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human TECTB |
| Epitope Specificity | 101-200/329 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SUBCELLULAR LOCATION | Cell membrane. Secreted; extracellular space; extracellular matrix. Found in the non-collagenous matrix of the tectorial membrane. |
| SIMILARITY | Contains 1 ZP domain. |
| SUBUNIT | May form homomeric filament after self-association or heteromeric filament after association with alpha-tectorin. |
| Post-translational modifications | The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | Beta-tectorin is a 329 amino acid secreted protein that contains one zona pellucida (ZP) domain. While it may form homomeric filaments after self-association, Beta-tectorin may also form heteromeric filaments when it associates with ?tectorin. The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia and proteolytically released into the extracellular compartment. Beta-tectorin is one of the major non-collagenous components of the tectorial membrane. The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. |
| Gene ID | 6975 |
|---|---|
| Other Names | Beta-tectorin, TECTB |
| Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=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. |
| Name | TECTB |
|---|---|
| Function | One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair- cell membrane potential, transducing sound into electrical signals. |
| Cellular Location | Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side. Secreted, extracellular space, extracellular matrix. Note=Found in the non- collagenous matrix of the tectorial membrane. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Beta-tectorin is a 329 amino acid secreted protein that contains one zona pellucida (ZP) domain. While it may form homomeric filaments after self-association, Beta-tectorin may also form heteromeric filaments when it associates with ?tectorin. The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia and proteolytically released into the extracellular compartment. Beta-tectorin is one of the major non-collagenous components of the tectorial membrane. The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals.
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