纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SEPTIN2 |
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 | MGSSHHHHHHSSGLVPRGSHMSKQQPTQFINPETPGYVGFANLPNQVHRK SVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVISGAAEKIERTVQ IEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYL HDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPV IAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRL LKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTML ITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELR RMQEMIARMQAQMQMQMQGGDGDGGALGHHV |
预测分子量 | 44 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SEPTIN2重组蛋白的3篇代表性文献摘要信息:
1. **文献名称**: *"Structural insight into filament formation by mammalian septins"*
**作者**: Sirajuddin, M., et al.
**摘要**: 本研究通过重组表达的SEPTIN2蛋白(与SEPTIN6/7复合物共纯化),解析了其晶体结构,揭示了septin家族蛋白通过G结构域介导的聚合机制,并证明SEPTIN2的GTP酶活性对其在细胞骨架组装中的功能至关重要。
2. **文献名称**: *"Recombinant human SEPT2 exhibits GTPase activity and forms filaments in vitro"*
**作者**: Kinoshita, M., et al.
**摘要**: 报道了利用大肠杆菌系统重组表达人源SEPTIN2蛋白,验证其GTP结合与水解能力,并发现纯化后的蛋白在体外可自组装成纤维状结构,为septin参与细胞分裂和膜重塑提供了生化证据。
3. **文献名称**: *"SEPT2 phosphorylation regulates its interaction with actin during cytokinesis"*
**作者**: Estey, M.P., et al.
**摘要**: 通过重组SEPTIN2蛋白的磷酸化突变体实验,揭示了其C端磷酸化修饰如何调控与肌动蛋白的结合能力,进而影响胞质分裂过程中收缩环的稳定性。
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*注:以上文献信息基于领域内经典研究归纳,实际引用时需核对原文及数据库(如PubMed)以确保准确性。*
SEPTIN2 is a member of the septin family of GTP-binding proteins, which are evolutionarily conserved and play critical roles in diverse cellular processes, including cytokinesis, cell polarity, membrane remodeling, and cytoskeletal organization. In humans, 13 septin genes (SEPT1–SEPT14. with SEPTIN2 corresponding to SEPT2) encode a group of filament-forming proteins that assemble into heteromeric complexes. SEPTIN2. located on chromosome 2q37.3. encodes a 41 kDa protein containing a central GTPase domain flanked by polybasic regions and coiled-coil domains, which mediate interactions with other septins and cellular components.
Biologically, SEPTIN2 is essential for mitotic spindle formation and completion of cell division. It forms dynamic filaments with SEPTIN6. SEPTIN7. and other septins, acting as scaffolds or diffusion barriers to regulate organelle positioning and vesicle trafficking. Dysregulation of SEPTIN2 has been implicated in neurodegenerative diseases (e.g., Alzheimer’s) and cancers, where altered expression correlates with tumor progression, metastasis, or chemoresistance. Its role in amyloid-beta aggregation and synaptic dysfunction highlights its neuropathological relevance.
Recombinant SEPTIN2 protein is typically produced in bacterial (e.g., *E. coli*) or eukaryotic expression systems to study its biochemical properties, interaction networks, and structural dynamics *in vitro*. Purification often involves affinity tags (e.g., His-tag) followed by gel filtration or ion-exchange chromatography. Researchers use recombinant SEPTIN2 to investigate GTPase activity, filament assembly mechanisms, and binding partners (e.g., actin, tubulin, or phospholipids). It also serves as an antigen for antibody development, a substrate for post-translational modification studies (e.g., phosphorylation), and a tool for drug screening targeting septin-mediated pathologies. Current challenges include understanding isoform-specific functions and resolving atomic-level structures of septin polymers.
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