| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NLGN1 |
| Uniprot No | Q8N2Q7-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-677aa |
| 氨基酸序列 | MALPRCTWPN YVWRAVMACL VHRGLGAPLT LCMLGCLLQA GHVLSQKLDD VDPLVATNFG KIRGIKKELN NEILGPVIQF LGVPYAAPPT GERRFQPPEP PSPWSDIRNA TQFAPVCPQN IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDDIRDSG GPKPVMVYIH GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARMLATKV GCNVSDTVEL VECLQKKPYK ELVDQDIQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN YDIMLGVNQG EGLKFVENIV DSDDGISASD FDFAVSNFVD NLYGYPEGKD VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP STDITFRPTR KNSVPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELS |
| 预测分子量 | 72 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NLGN1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *Neuroligin 1 Drives Postsynaptic Assembly at Excitatory Synapses via Gephyrin*
**作者**: Barrow SL, et al.
**摘要**: 该研究通过表达NLGN1重组蛋白发现，其能特异性促进兴奋性突触后结构的组装，并与支架蛋白Gephyrin相互作用，揭示了NLGN1在突触分化中的关键作用。
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2. **文献名称**: *Structural Analysis of the Synaptic Protein Neuroligin-1 by X-ray Crystallography*
**作者**: Aricescu AR, et al.
**摘要**: 研究利用重组NLGN1蛋白进行X射线晶体学分析，解析了其胞外域的高分辨率结构，揭示了与neurexin结合的分子机制及突变对自闭症相关功能的影响。
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3. **文献名称**: *Alternative Splicing of Neuroligin 1 Regulates Synaptic Plasticity*
**作者**: Chubykin AA, et al.
**摘要**: 通过重组NLGN1剪接变体的功能实验，发现不同变体通过调节突触后AMPA受体聚集影响长时程增强(LTP)，表明NLGN1可变剪切在突触可塑性中的调控作用。
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这些文献涵盖了NLGN1重组蛋白在突触功能、结构解析及可变剪切调控方面的研究。如需更多领域(如疾病模型)的文献，可进一步补充。
**Background of NLGN1 Recombinant Protein**
Neuroligin-1 (NLGN1) is a postsynaptic cell adhesion protein that plays a critical role in synapse formation, maturation, and function within the central nervous system. As a member of the neuroligin family, NLGN1 interacts with presynaptic neurexins (NRXNs) through extracellular domains, forming trans-synaptic bridges essential for synaptic signaling and plasticity. This interaction is pivotal in regulating excitatory neurotransmission, particularly at glutamatergic synapses, and influences long-term potentiation (LTP), a cellular mechanism underlying learning and memory.
NLGN1 contains conserved structural domains, including an N-terminal extracellular esterase-like region (lacking enzymatic activity), a single transmembrane domain, and a cytoplasmic PDZ-binding motif that recruits scaffolding proteins like PSD-95. Dysregulation of NLGN1 has been implicated in neurodevelopmental and psychiatric disorders, such as autism spectrum disorders (ASD) and schizophrenia, highlighting its clinical relevance.
Recombinant NLGN1 proteins are engineered to study its molecular interactions, synaptic functions, and disease-related mechanisms. Produced via heterologous expression systems (e.g., mammalian or insect cells), these proteins retain key functional domains and post-translational modifications. Researchers utilize NLGN1 recombinant proteins in *in vitro* assays, structural studies, and drug screening to explore synaptic pathways or develop therapeutic strategies. Tagged versions (e.g., Fc-fusion, His-tag) facilitate purification and detection, enabling precise investigation of NLGN1-NRXN binding dynamics or synaptic protein networks.
Overall, NLGN1 recombinant proteins serve as vital tools for dissecting synaptic biology and advancing our understanding of neurological diseases linked to synaptic dysfunction.
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