| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEC6L1 |
| Uniprot No | O60645 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-756 aa |
| 活性数据 | MQCEDSTSFF TMKETDREAV ATAVQRVAGM LQRPDQLDKV EQYRRREARK KASVEARLKA AIQSQLDGVR TGLSQLHNAL NDVKDIQQSL ADVSKDWRQS INTIESLKDV KDAVVQHSQL AAAVENLKNI FSVPEIVRET QDLIEQGALL QAHRKLMDLE CSRDGLMYEQ YRMDSGNTRD MTLIHGYFGS TQGLSDELAK QLWMVLQRSL VTVRRDPTLL VSVVRIIERE EKIDRRILDR KKQTGFVPPG RPKNWKEKMF TILERTVTTR IEGTQADTRE SDKMWLVRHL EIIRKYVLDD LIVAKNLMVQ CFPPHYEIFK NLLNMYHQAL STRMQDLASE DLEANEIVSL LTWVLNTYTS TEMMRNVELA PEVDVGTLEP LLSPHVVSEL LDTYMSTLTS NIIAWLRKAL ETDKKDWVKE TEPEADQDGY YQTTLPAIVF QMFEQNLQVA AQISEDLKTK VLVLCLQQMN SFLSRYKDEA QLYKEEHLRN RQHPHCYVQY MIAIINNCQT FKESIVSLKR KYLKNEVEEG VSPSQPSMDG ILDAIAKEGC SGLLEEVFLD LEQHLNELMT KKWLLGSNAV DIICVTVEDY FNDFAKIKKP YKKRMTAEAH RRVVVEYLRA VMQKRISFRS PEERKEGAEK MVREAEQLRF LFRKLASGFG EDVDGYCDTI VAVAEVIKLT DPSLLYLEVS TLVSKYPDIR DDHIGALLAV RGDASRDMKQ TIMETLEQGP AQASPSYVPL FKDIVVPSLN VAKLLK |
| 分子量 | 85.5 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. |
以下是关于重组人SEC6L1蛋白的参考文献示例，包含文献名称、作者及摘要内容概述：
1. **文献名称**：*"Expression and Functional Analysis of Recombinant Human SEC6L1 in Exocytosis"*
**作者**：Smith J. et al.
**摘要**：本研究在哺乳动物细胞中成功表达了重组人SEC6L1蛋白，并验证其与exocyst复合体的相互作用。实验表明SEC6L1在细胞分泌过程中调控囊泡锚定，影响胞吐作用效率。
2. **文献名称**：*"Purification and Characterization of the Human Exocyst Component SEC6L1"*
**作者**：Johnson R. et al.
**摘要**：利用昆虫细胞表达系统规模化生产重组SEC6L1蛋白，通过亲和层析纯化后，结合质谱和晶体学分析其结构，揭示了其在exocyst复合体中的关键结构域。
3. **文献名称**：*"SEC6L1 Mediates Vesicle Docking in Neuronal Synapses"*
**作者**：Brown L. et al.
**摘要**：通过体外重组SEC6L1蛋白实验，证明其与神经元突触前膜蛋白(如Syntaxin)结合，调控突触囊泡的运输与神经递质释放，提示其在神经信号传导中的作用。
4. **文献名称**：*"Role of Recombinant SEC6L1 in Cancer Cell Migration and Invasion"*
**作者**：Lee S. et al.
**摘要**：研究发现，重组SEC6L1蛋白可通过调节exocyst复合体活性，影响癌细胞的迁移能力，为靶向肿瘤转移提供了潜在分子靶点。
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**备注**：以上文献为假设示例，实际检索时建议通过PubMed、Google Scholar等平台，结合关键词“recombinant SEC6L1”“EXOC4 protein”“exocyst complex”进一步验证。若研究较少，可扩展至exocyst复合体其他组分(如SEC8、EXOC2)的相关文献。
**Background of Recombinant Human SEC6L1 Protein**
SEC6L1 (Secretory 6 Homolog Like 1), a member of the exocyst complex, plays a critical role in intracellular vesicle trafficking and exocytosis. This protein is involved in tethering secretory vesicles to the plasma membrane, facilitating cargo release during processes like cell polarization, cytokinesis, and neurotransmitter secretion. Structurally, it contains conserved domains enabling interactions with other exocyst subunits (e.g., SEC3. SEC5) and regulatory proteins, linking vesicle transport to cellular signaling pathways.
Recombinant human SEC6L1 protein is engineered through heterologous expression systems (e.g., E. coli, mammalian cells) to study its biochemical functions and mechanisms. Its production enables in vitro analyses, such as binding assays, structural studies, and screening for molecular interactions. Research highlights its involvement in pathologies: dysregulated SEC6L1 expression correlates with cancers (e.g., breast, colorectal) by affecting metastasis-related secretion, and neurodegenerative disorders, where impaired exocytosis disrupts synaptic function. Additionally, SEC6L1 interacts with GTPases (e.g., RalA, Rho) and cytoskeletal components, suggesting roles in cell migration and invasion.
Current studies focus on SEC6L1’s potential as a therapeutic target, leveraging recombinant proteins to dissect its role in disease pathways or drug responsiveness. Further exploration of its post-translational modifications and tissue-specific isoforms could deepen understanding of exocyst complex diversity in health and disease.
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