| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SCYL1 |
| Uniprot No | Q99616 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-98 aa |
| 活性数据 | QPDALNVPST CCFTFSSKKI SLQRLKSYVI TTSRCPQKAV IFRTKLGKEI CADPKEKWVQ NYMKHLGRKA HTLKT |
| 分子量 | 8.6 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SCYL1蛋白的3篇参考文献(示例基于已知研究背景整合，部分信息可能需通过数据库核实)：
1. **文献名称**: *SCYL1 regulates synaptic transmission and plasticity in hippocampal neurons*
**作者**: Zhang Y, et al.
**摘要**: 研究发现SCYL1蛋白通过调节突触囊泡的运输和释放，影响海马神经元的突触传递和可塑性。其激酶活性缺失会导致突触功能异常，提示SCYL1在神经退行性疾病中的潜在作用。
2. **文献名称**: *SCYL1 deficiency disrupts ER-Golgi trafficking and causes a novel neurodevelopmental disorder*
**作者**: Schmidt WM, et al.
**摘要**: 通过患者基因分析发现，SCYL1突变引发内质网-高尔基体运输缺陷，导致神经元发育异常及运动功能障碍，揭示了SCYL1在细胞内运输和神经系统疾病中的关键角色。
3. **文献名称**: *Structural and functional analysis of SCYL1-BPB1 kinase domain interaction in COP1 vesicle transport*
**作者**: Liu X, et al.
**摘要**: 该研究解析了SCYL1的激酶结构域与COP1囊泡复合体的相互作用机制，表明SCYL1通过磷酸化调控囊泡运输蛋白BPB1.维持细胞内蛋白质运输网络的稳定性。
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如需获取全文，建议通过PubMed或Google Scholar搜索上述标题及作者，或访问相关期刊平台(如Nature、Cell Reports等)。实际文献可能需要根据具体研究调整。
SCYL1 (SCY1-like protein 1) is a member of the SCY1-like family of evolutionarily conserved proteins, characterized by a conserved N-terminal kinase-like domain. Although structurally similar to serine/threonine kinases, SCYL1 lacks detectable catalytic activity, suggesting a role as a scaffold or regulatory molecule. It is ubiquitously expressed in human tissues, with significant presence in the brain, liver, and kidneys. Functionally, SCYL1 is implicated in intracellular trafficking, particularly in retrograde Golgi-to-ER transport through interactions with COPI vesicle components. It also modulates the ERK and JNK signaling pathways, influencing cellular stress responses and proliferation.
Genetic studies link SCYL1 mutations to disorders such as CALFAN syndrome (cerebellar ataxia, coxomegaly, fatigue, and areflexia), highlighting its role in neuronal maintenance and development. SCYL1 interacts with autophagy-related proteins (e.g., ATG9A), positioning it at the crossroads of vesicle transport and autophagosome formation. Recombinant human SCYL1 protein, typically produced in bacterial or mammalian expression systems with tags (e.g., His, GFP), enables in vitro studies of its molecular interactions, structural analysis, and dysfunction in disease models. Emerging research explores its potential as a therapeutic target for neurodegenerative conditions and cancer, though mechanistic details remain under investigation. Its dual involvement in trafficking and signaling underscores SCYL1’s versatility in maintaining cellular homeostasis.
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