| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SYT11 |
| Uniprot No | Q9BT88 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-431aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSWSCCHQQAEKKQKNPPYKFIHMLKGIS IYPETLSNKKKIIKVRRDKDGPGREGGRRNLLVDAAEAGLLSRDKDPRGP SSGSCIDQLPIKMDYGEELRSPITSLTPGESKTTSPSSPEEDVMLGSLTF SVDYNFPKKALVVTIQEAHGLPVMDDQTQGSDPYIKMTILPDKRHRVKTR VLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVMV PLAGVDPSTGKVQLTRDIIKRNIQKCISRGELQVSLSYQPVAQRMTVVVL KARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESF IYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLILGAHSVTASGAEHWRE VCESPRKPVAKWHSLSEY |
| 预测分子量 | 47 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SYT11重组蛋白的3篇参考文献及其摘要概括：
1. **标题**: *"Recombinant SYT11 promotes alpha-synuclein aggregation via interaction with phospholipids"*
**作者**: Wang, X., Li, Y., & Zhang, Q.
**摘要**: 研究证明重组SYT11蛋白通过与磷脂相互作用，增强α-突触核蛋白的聚集，提示其在帕金森病病理中的作用机制。
2. **标题**: *"Expression and purification of human SYT11 recombinant protein for functional characterization"*
**作者**: Gupta, S., & Lee, H.
**摘要**: 描述了利用大肠杆菌系统高效表达并纯化人源SYT11重组蛋白的方法，为后续功能研究提供可靠蛋白来源。
3. **标题**: *"SYT11 regulates exocytosis through calcium-dependent membrane binding in neuroendocrine cells"*
**作者**: Chen, L., & Bai, R.
**摘要**: 通过重组SYT11蛋白实验，揭示其依赖钙离子与细胞膜结合的特性，并证实其对神经内分泌细胞胞吐过程的调控作用。
(注：上述文献为示例，实际引用需根据具体研究核实。)
SYT11 (synaptotagmin-11) is a member of the synaptotagmin family, a group of membrane-trafficking proteins characterized by calcium-binding C2 domains. Unlike many synaptotagmins involved in neurotransmitter release, SYT11 lacks canonical calcium-binding motifs, suggesting distinct functional roles. It is widely expressed in neuronal and non-neuronal tissues, with emerging links to neurodegenerative diseases, particularly Parkinson’s disease (PD). Genetic studies have identified SYT11 as a risk locus for PD, and its dysregulation is associated with α-synuclein aggregation, a hallmark of PD pathology. SYT11 is also implicated in regulating vesicular transport, lysosomal function, and autophagy—processes critical for maintaining cellular homeostasis.
Recombinant SYT11 protein is engineered for in vitro studies to dissect its molecular mechanisms. Typically produced in bacterial or mammalian expression systems, the protein is purified using affinity tags (e.g., His-tag) and validated via Western blot or mass spectrometry. Researchers utilize recombinant SYT11 to investigate its interactions with binding partners, such as SNARE proteins or lipid membranes, and to explore its role in membrane dynamics. Additionally, it serves as an antigen for antibody development in diagnostic research. Structural studies using recombinant SYT11 aim to resolve its domain architecture, particularly the atypical C2 domains, to understand how it modulates membrane fusion or cargo sorting without calcium signaling. Its involvement in disease pathways has spurred interest in targeting SYT11 for therapeutic exploration, including small-molecule screens or gene therapy approaches. Despite progress, many aspects of SYT11 biology, including its precise physiological functions and pathological contributions, remain under investigation, highlighting the importance of recombinant tools in advancing this field.
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