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Recombinant Human SNX17 protein

  • 中文名: 分拣连接蛋白17(SNX17)重组蛋白
  • 别    名: SNX17;KIAA0064;Sorting nexin-17
货号: PA1000-8381
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点SNX17
Uniprot No Q15036
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-470aa
氨基酸序列MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVLPAFP PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIERGWILVT KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGSTSSPGRG RGEVRLELAF EYLMSKDRLQ WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE SPDATRESMV KLSSKLSAVS LRGIGSPSTD ASASDVHGNF AFEGIGDEDL
预测分子量kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是关于SNX17重组蛋白的3篇参考文献示例(内容基于公开研究整理,非真实文献):

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1. **文献名称**: *SNX17 mediates PDZ-directed sorting from endosomes to the TGN*

**作者**: Ghai R., et al.

**摘要**: 本研究揭示了SNX17通过其PDZ结构域识别特定胞内受体(如LDLR和β1-integrin),调控它们从内体到反式高尔基体的逆向运输过程。重组SNX17蛋白的实验证实其通过膜结合能力参与运输复合体组装。

2. **文献名称**: *Structural basis for SNX17’s role in cargo recycling*

**作者**: Steinberg F., et al.

**摘要**: 通过X射线晶体学解析了SNX17重组蛋白的PX和FERM结构域三维结构,发现其通过独特的构象变化结合磷脂酰肌醇3-磷酸(PI3P)和整合素尾部,阐明了其在胞吞循环中的分子机制。

3. **文献名称**: *SNX17 interacts with retromer to prevent lysosomal degradation of Wntless*

**作者**: Zhang P., et al.

**摘要**: 研究证明重组SNX17蛋白与retromer复合体协作,通过稳定Wntless蛋白在早期内体的定位,调控Wnt信号通路。缺失SNX17导致Wntless异常降解,影响胚胎发育。

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**注**:以上为模拟文献,实际引用请通过PubMed/Google Scholar检索关键词如“SNX17 recombinant protein”、“SNX17 structure function”获取真实文献。

背景信息

SNX17 (Sorting Nexin 17) is a member of the sorting nexin family, a group of proteins characterized by their ability to bind phosphoinositides via a conserved Phox homology (PX) domain. These proteins play critical roles in membrane trafficking, endosomal sorting, and cellular signaling. SNX17 is distinguished by its unique structural features, including a C-terminal FERM (Four-point-one, Ezrin, Radixin, Moesin) domain, which enables interactions with cytoskeletal components and transmembrane proteins, such as integrins and lipoprotein receptors. This dual-domain architecture allows SNX17 to act as a molecular scaffold, coordinating cargo recognition, vesicle formation, and intracellular transport.

Functionally, SNX17 is implicated in regulating the endocytic recycling of key receptors, notably low-density lipoprotein receptor (LDLR) and β1-integrins, by facilitating their retrieval from endosomes to the trans-Golgi network or plasma membrane. This process is vital for maintaining cellular homeostasis, receptor signaling, and cell adhesion. Dysregulation of SNX17 has been linked to cardiovascular diseases, neurodegeneration, and cancer metastasis, underscoring its physiological relevance.

Recombinant SNX17 protein is engineered for in vitro studies to dissect its molecular interactions, structural dynamics, and role in trafficking pathways. Typically produced in bacterial or mammalian expression systems, it retains functional domains for binding assays, structural biology (e.g., crystallography), or reconstituting transport mechanisms in cell-free systems. Tagged versions (e.g., His-tag, GST-tag) enable purification and detection. Research leveraging recombinant SNX17 has advanced understanding of endosomal sorting machinery and its potential as a therapeutic target for trafficking-related disorders. Its application extends to drug screening platforms and mechanistic studies of receptor regulation.

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