| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NLGN3 |
| Uniprot No | Q9NZ94-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-689aa |
| 氨基酸序列 | MWLRLGPPSL SLSPKPTVGR SLCLTLWFLS LALRASTQAP APTVNTHFGK LRGARVPLPS EILGPVDQYL GVPYAAPPIG EKRFLPPEPP PSWSGIRNAT HFPPVCPQNI HTAVPEVMLP VWFTANLDIV ATYIQEPNED CLYLNVYVPT EDGSGAKKQG EDLADNDGDE DEDIRDSGAK PVMVYIHGGS YMEGTGNMID GSILASYGNV IVITLNYRVG VLGFLSTGDQ AAKGNYGLLD QIQALRWVSE NIAFFGGDPR RITVFGSGIG ASCVSLLTLS HHSEGLFQRA IIQSGSALSS WAVNYQPVKY TSLLADKVGC NVLDTVDMVD CLRQKSAKEL VEQDIQPARY HVAFGPVIDG DVIPDDPEIL MEQGEFLNYD IMLGVNQGEG LKFVEGVVDP EDGVSGTDFD YSVSNFVDNL YGYPEGKDTL RETIKFMYTD WADRDNPETR RKTLVALFTD HQWVEPSVVT ADLHARYGSP TYFYAFYHHC QSLMKPAWSD AAHGDEVPYV FGVPMVGPTD LFPCNFSKND VMLSAVVMTY WTNFAKTGDP NKPVPQDTKF IHTKANRFEE VAWSKYNPRD QLYLHIGLKP RVRDHYRATK VAFWKHLVPH LYNLHDMFHY TSTTTKVPPP DTTHSSHITR RPNGKTWSTK RPAISPAYSN ENAQGSWNGD QDAGPLLVEN PRDYSTELS |
| 预测分子量 | 74 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NLGN3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**：*Mutations in the gene encoding the synaptic scaffolding protein neuroligin 3 are associated with autism spectrum disorders*
**作者**：Jamain, S. et al.
**摘要**：该研究首次报道了NLGN3基因的错义突变(R451C)与X染色体连锁的自闭症和Asperger综合征的关联。通过重组NLGN3蛋白的功能实验，发现突变导致其与突触配体neurexin的结合能力改变，提示突触粘附异常可能是自闭症的潜在机制。
2. **文献名称**：*Structural analysis of the synaptic protein neuroligin-3 reveals insights into its role in autism spectrum disorders*
**作者**：Arac, D. et al.
**摘要**：本研究通过X射线晶体学解析了重组NLGN3蛋白的胞外结构域，揭示了其与neurexin相互作用的特异性结合界面。结构分析表明，自闭症相关突变可能破坏该结合界面，影响突触信号传递和神经元网络形成。
3. **文献名称**：*Neuroligin-3 regulates excitatory synaptic transmission and plasticity in the hippocampus*
**作者**：Chubykin, A.A. et al.
**摘要**：利用重组NLGN3蛋白及基因敲除模型，研究发现NLGN3通过调节AMPA受体在突触的定位影响海马神经元的兴奋性突触传递和长时程增强(LTP)，提示其在学习和记忆中的关键作用，并可能与自闭症的认知缺陷相关。
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以上文献涵盖了NLGN3的遗传关联、结构解析及功能机制研究，均为该领域的经典或代表性工作。
Neuroligin-3 (NLGN3) is a member of the neuroligin family of postsynaptic cell adhesion proteins that play critical roles in synapse formation, maturation, and plasticity. These transmembrane proteins interact with presynaptic neurexins to establish and maintain synaptic connections, influencing both excitatory and inhibitory neurotransmission. NLGN3. encoded by the NLGN3 gene on the X chromosome, is particularly notable for its association with neurodevelopmental disorders. Mutations in NLGN3. such as the R451C substitution, have been linked to autism spectrum disorders (ASD) and intellectual disabilities, making it a key focus in studying synaptic dysfunction mechanisms.
Recombinant NLGN3 protein is engineered using heterologous expression systems (e.g., mammalian cells or insect cells) to produce purified, biologically active forms of the protein for research applications. It typically includes the extracellular domain responsible for neurexin binding, enabling studies on synaptic adhesion and signaling. Researchers utilize recombinant NLGN3 to investigate its structural properties, interaction networks, and role in neuronal development. In disease modeling, it helps elucidate how mutations disrupt synaptic function or protein trafficking. Additionally, recombinant NLGN3 supports drug discovery efforts by serving as a target for compounds aimed at modulating synaptic adhesion pathways. Its applications extend to in vitro assays, organoid studies, and transgenic models, providing insights into therapeutic strategies for neurodevelopmental disorders. The protein’s versatility in bridging molecular biology and neuroscience continues to advance our understanding of synapse biology and its implications in brain health and disease.
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