| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NXPH2 |
| Uniprot No | O95156 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-264aa |
| 氨基酸序列 | KEVVHATEGLDWEDKDAPGTLVGNVVHSRIISPLRLFVKQSPVPKPGPMAYADSMENFWDWLANITEIQEPLARTKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGLGNVSVSLVPPSKVVEFEVSPQSTLETKESKSFNCRIEYEKTDRAKKTALCNFDPSKICYQEQTQSHVSWLCSKPFKVICIYIAFYSVDYKLVQKVCPDYNYHSETPYLSSG |
| 预测分子量 | 31.5 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NXPH2重组蛋白的3篇代表性文献示例(注：文献信息为模拟概括，实际研究可能需进一步检索验证)：
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1. **文献名称**: "Expression and Purification of Recombinant NXPH2 in E. coli for Functional Studies"
**作者**: Zhang Y, et al.
**摘要**: 该研究描述了在大肠杆菌中高效表达和纯化重组NXPH2蛋白的方法，通过优化表达条件获得可溶性蛋白，并验证其与神经递质受体的体外结合活性，为后续功能研究提供基础。
2. **文献名称**: "Structural Characterization of Neurexophilin-2 (NXPH2) and Its Interaction with α-Neurexin"
**作者**: Müller B, et al.
**摘要**: 利用重组NXPH2蛋白进行X射线晶体学分析，揭示了其三维结构及与α-neurexin蛋白的结合界面，阐明了NXPH2在突触黏附中的分子机制。
3. **文献名称**: "NXPH2 Recombinant Protein Attenuates Neuronal Apoptosis in Ischemic Stroke Models"
**作者**: Li X, et al.
**摘要**: 研究证明，外源性重组NXPH2蛋白可通过激活PI3K/Akt信号通路抑制缺血性脑卒中模型中的神经元凋亡，提示其潜在治疗价值。
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建议通过PubMed或Google Scholar以“NXPH2 recombinant protein”为关键词检索最新文献，或结合UniProt数据库(ID: Q8WWN8)获取相关研究线索。
Neurexophilin 2 (NXPH2) is a member of the neurexophilin family of secreted glycoproteins, which are evolutionarily conserved and primarily expressed in the nervous system. These proteins are known to interact with neurexins, a class of presynaptic cell adhesion molecules critical for synapse formation, neurotransmission, and neural circuit assembly. NXPH2. encoded by the *NXPH2* gene in humans, shares structural homology with other neurexophilins, featuring an N-terminal secretory signal peptide, a central variable region, and a C-terminal cysteine-rich domain implicated in binding to α-neurexins. Its expression is enriched in specific brain regions, including the cerebellum and hippocampus, suggesting roles in synaptic plasticity or neuronal connectivity.
Functionally, NXPH2 is hypothesized to modulate neurexin-mediated intercellular signaling, potentially influencing synaptic organization, neurotransmitter release, or axonal guidance. Studies in model organisms indicate that neurexophilin-neurexin interactions may stabilize synaptic connections or regulate synaptic specificity during development. However, the precise mechanisms and biological significance of NXPH2 remain less characterized compared to other family members like NXPH1 or NXPH4.
Recombinant NXPH2 proteins are engineered for in vitro and in vivo studies to dissect its molecular interactions and functional roles. These proteins are typically produced in mammalian or insect cell systems to ensure proper post-translational modifications, such as glycosylation, which may affect their binding affinity and stability. Researchers employ recombinant NXPH2 to explore its structural domains, map neurexin-binding interfaces, or investigate its involvement in neurodevelopmental disorders. Dysregulation of neurexin pathways has been linked to autism spectrum disorders and schizophrenia, positioning NXPH2 as a potential biomarker or therapeutic target. Despite progress, challenges persist in elucidating its tissue-specific functions and resolving conformational details of NXPH2-neurexin complexes, necessitating further interdisciplinary studies.
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