| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SYNGR1 |
| Uniprot No | O43759 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-191aa |
| 氨基酸序列 | MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWSLTAALAVRRFKDLSFQEEYSTLFPASAQP |
| 预测分子量 | 48.0 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SYNGR1重组蛋白的模拟参考文献示例(注：内容为虚构，仅用于示例用途)：
1. **文献名称**: "Recombinant SYNGR1 Protein Expression and Its Role in Neuronal Vesicle Trafficking"
**作者**: Zhang L, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化了SYNGR1重组蛋白，证实其可调控神经元突触囊泡的运输，并揭示了其与突触结合蛋白的相互作用机制。
2. **文献名称**: "Structural Characterization of Human SYNGR1 Using Cryo-EM"
**作者**: Müller R, et al.
**摘要**: 利用冷冻电镜解析了SYNGR1重组蛋白的三维结构，发现其跨膜结构域对维持突触膜稳定性至关重要，为神经退行性疾病研究提供新靶点。
3. **文献名称**: "SYNGR1 Recombinant Protein Enhances Axonal Regeneration in vitro"
**作者**: Tanaka K, et al.
**摘要**: 在哺乳动物细胞中表达SYNGR1重组蛋白，证明其通过激活PI3K/AKT通路促进受损轴突再生，提示其在神经修复中的潜在应用价值。
4. **文献名称**: "Interactome Analysis of SYNGR1 in Parkinson’s Disease Models"
**作者**: Gupta S, et al.
**摘要**: 通过重组SYNGR1蛋白筛选相互作用蛋白网络，发现其与α-突触核蛋白的异常关联可能参与帕金森病的病理进程。
(注：以上文献为模拟生成，实际研究中请通过PubMed、Google Scholar等平台检索真实文献。)
SYNGR1 (Synaptogyrin-1) is a member of the synaptogyrin family, a group of integral membrane proteins predominantly localized to synaptic vesicles and other intracellular membrane compartments. Initially identified in neuronal tissues, it plays a role in modulating synaptic vesicle dynamics, neurotransmitter release, and synaptic plasticity. Structurally, SYNGR1 contains four transmembrane domains, with both N- and C-termini oriented toward the cytoplasm, facilitating interactions with cytosolic proteins involved in vesicle trafficking. Its expression is not restricted to neurons; non-neuronal cells, including immune cells and certain cancer types, also exhibit SYNGR1 activity, suggesting broader physiological and pathological roles.
Research links SYNGR1 to neurological disorders, such as schizophrenia and neurodegenerative diseases, where altered expression or mutations correlate with synaptic dysfunction. In cancer, SYNGR1 has been implicated in tumor progression, metastasis, and chemoresistance, though its mechanisms remain under investigation. For instance, it may regulate cell adhesion, membrane receptor internalization, or signaling pathways like EGFR or Wnt/β-catenin.
Recombinant SYNGR1 protein is typically produced using bacterial, insect, or mammalian expression systems, often tagged for purification and detection (e.g., His, GFP). This engineered protein enables in vitro studies to dissect its biochemical properties, binding partners, and structural motifs. Applications include probing its role in vesicle fusion assays, screening for interacting drugs, or analyzing post-translational modifications. In cellular models, recombinant SYNGR1 helps elucidate its impact on membrane trafficking, apoptosis, or oncogenic signaling. While therapeutic targeting remains exploratory, understanding SYNGR1's molecular interactions could inform strategies for neurological or oncology treatments. Current challenges include clarifying isoform-specific functions and resolving conflicting data across different experimental systems.
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