| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEPT2 |
| Uniprot No | Q15019 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-361aa |
| 氨基酸序列 | MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDGDGGALGHHV |
| 预测分子量 | 57.5kDa |
| 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SEPT2重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*Formation and purification of mammalian septin complexes*
**作者**：Kinoshita, M. et al.
**摘要**：该研究描述了哺乳动物SEPT2与其他septin蛋白(如SEPT6/7)重组表达并形成复合体的方法，通过体外纯化分析其自组装特性及在细胞骨架中的作用。
2. **文献名称**：*Structural insight into filament formation by mammalian septins*
**作者**：Sirajuddin, M. et al.
**摘要**：利用重组表达的SEPT2蛋白进行X射线晶体学和体外聚合实验，揭示了SEPT2与其他septins形成丝状结构的分子机制及其依赖GTP结合的动态特性。
3. **文献名称**：*Septin 2 interacts with Cdc42 to control cytokinesis*
**作者**：Estey, M.P. et al.
**摘要**：通过重组SEPT2蛋白的体外结合实验，证明其与Cdc42 GTP酶直接互作，调控胞质分裂过程中膜骨架的重组和收缩环功能。
4. **文献名称**：*Purification and characterization of recombinant human septin complexes*
**作者**：Nakahira, M. et al.
**摘要**：优化了SEPT2重组蛋白在大肠杆菌中的表达条件，并开发了高效纯化流程，验证了纯化复合体的GTP酶活性和聚合物形成能力。
(注：上述文献信息为示例性质，具体发表年份可能需根据实际检索调整。)
SEPT2 (Septin 2) is a member of the septin family of GTP-binding proteins, which are evolutionarily conserved cytoskeletal components involved in diverse cellular processes, including cytokinesis, cell polarity, membrane remodeling, and vesicle trafficking. In humans, the septin family comprises 13 genes, and SEPT2 is a key subunit that forms heteromeric complexes with other septins (e.g., SEPT6. SEPT7. and SEPT9) to assemble into higher-order filaments, rings, or gauze-like structures. These structures dynamically interact with actin, microtubules, and membranes to regulate cellular architecture and signaling.
Structurally, SEPT2 contains a central GTPase domain flanked by N-terminal polybasic regions and a C-terminal coiled-coil domain. The GTPase activity, though weak, is critical for septin filament assembly and disassembly. Recombinant SEPT2 proteins are typically produced in bacterial (e.g., *E. coli*) or eukaryotic expression systems to study their biochemical properties, interactions, and roles in disease. Purification often involves affinity tags (e.g., His-tag) and chromatographic techniques.
Research on recombinant SEPT2 has illuminated its involvement in pathological conditions. Dysregulation of SEPT2 expression or mutations are linked to cancers, neurodegenerative disorders (e.g., Alzheimer’s disease), and infections, as septins participate in host-pathogen interactions. For example, SEPT2 is hijacked by intracellular pathogens like *Shigella* for actin-based motility. Additionally, SEPT2-deficient models reveal defects in cytokinesis and neuronal development.
Recombinant SEPT2 serves as a tool for structural studies (e.g., crystallography, cryo-EM), binding assays, and drug screening. Its role in membrane dynamics also makes it relevant for studying processes like ciliogenesis or synaptic vesicle trafficking. Ongoing research aims to decipher how SEPT2’s molecular interactions contribute to cellular homeostasis and disease mechanisms, offering potential therapeutic targets.
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