| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRRTM4 |
| Uniprot No | Q86VH4-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-424aa |
| 氨基酸序列 | MGFHLITQLK GMSVVLVLLP TLLLVMLTGA QRACPKNCRC DGKIVYCESH AFADIPENIS GGSQGLSLRF NSIQKLKSNQ FAGLNQLIWL YLDHNYISSV DEDAFQGIRR LKELILSSNK ITYLHNKTFH PVPNLRNLDL SYNKLQTLQS EQFKGLRKLI ILHLRSNSLK TVPIRVFQDC RNLDFLDLGY NRLRSLSRNA FAGLLKLKEL HLEHNQFSKI NFAHFPRLFN LRSIYLQWNR IRSISQGLTW TWSSLHNLDL SGNDIQGIEP GTFKCLPNLQ KLNLDSNKLT NISQETVNAW ISLISITLSG NMWECSRSIC PLFYWLKNFK GNKESTMICA GPKHIQGEKV SDAVETYNIC SEVQVVNTER SHLVPQTPQK PLIIPRPTIF KPDVTQSTFE TPSPSPGFQI PGAEQEYEHV SFHK |
| 预测分子量 | 47 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. |
以下是与LRRTM4重组蛋白相关的3篇文献示例：
1. **"LRRTM4 regulates excitatory synapse formation through recruitment of presynaptic NMDARs"**
- Authors: A. Sando, T. Südhof
- 摘要：研究通过重组LRRTM4蛋白发现其通过与突触前膜NMDA受体结合，调控兴奋性突触的形成和功能，揭示其在神经环路组装中的作用机制。
2. **"Structural basis of LRRTM4-neurexin interaction in synaptic adhesion"**
- Authors: K. Um et al.
- 摘要：利用重组LRRTM4胞外结构域解析其与轴突蛋白neurexin的复合物晶体结构，阐明两者结合的特异性及其对突触黏附的分子基础。
3. **"LRRTM4 modulates hippocampal plasticity and memory via glutamatergic signaling"**
- Authors: J. Roppongi et al.
- 摘要：通过体外重组LRRTM4功能实验，证明其通过调控谷氨酸能突触传递影响海马突触可塑性和记忆形成，提示其在认知障碍疾病中的潜在作用。
(注：以上为模拟文献，实际研究中建议通过PubMed或Google Scholar以关键词“LRRTM4 recombinant”检索近期论文。)
LRRTM4 (Leucine-Rich Repeat Transmembrane Protein 4) is a member of the LRRTM family, a group of synaptic cell adhesion molecules predominantly expressed in the nervous system. These proteins are characterized by extracellular leucine-rich repeat (LRR) domains, which mediate protein-protein interactions, and a single transmembrane domain followed by a short cytoplasmic tail. LRRTM4 is specifically enriched in excitatory synapses and has been implicated in synaptogenesis, synaptic plasticity, and neural circuit development. It interacts with presynaptic partners like neuroligins and heparan sulfate proteoglycans to regulate synapse formation and function. Notably, LRRTM4 shows preferential expression in the hippocampus and cerebral cortex, brain regions critical for learning and memory.
Recombinant LRRTM4 protein, produced via heterologous expression systems (e.g., mammalian or insect cells), retains the functional extracellular LRR domain, enabling studies of its binding properties and signaling mechanisms. Research highlights its role in recruiting postsynaptic scaffolding proteins through its cytoplasmic PDZ-binding motif, influencing AMPA receptor trafficking and synaptic strength. Dysregulation of LRRTM4 has been linked to neurodevelopmental disorders, including schizophrenia and autism spectrum disorders, as well as neurodegenerative conditions like Alzheimer’s disease. Its genetic variants are associated with altered synaptic connectivity and cognitive deficits in model organisms.
Recombinant LRRTM4 is widely used in vitro to investigate synapse biology, screen for small-molecule modulators, and develop therapeutic antibodies targeting synaptic adhesion pathways. However, challenges remain in fully elucidating its context-dependent interactions and disease-related mechanisms. Current studies focus on its crosstalk with other synaptic organizers and potential as a biomarker or drug target for neurological disorders.
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