| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FLRT2 |
| Uniprot No | O43155 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-539aa |
| 氨基酸序列 | MGLQTTKWPS HGAFFLKSWL IISLGLYSQV SKLLACPSVC RCDRNFVYCN ERSLTSVPLG IPEGVTVLYL HNNQINNAGF PAELHNVQSV HTVYLYGNQL DEFPMNLPKN VRVLHLQENN IQTISRAALA QLLKLEELHL DDNSISTVGV EDGAFREAIS LKLLFLSKNH LSSVPVGLPV DLQELRVDEN RIAVISDMAF QNLTSLERLI VDGNLLTNKG IAEGTFSHLT KLKEFSIVRN SLSHPPPDLP GTHLIRLYLQ DNQINHIPLT AFSNLRKLER LDISNNQLRM LTQGVFDNLS NLKQLTARNN PWFCDCSIKW VTEWLKYIPS SLNVRGFMCQ GPEQVRGMAV RELNMNLLSC PTTTPGLPLF TPAPSTASPT TQPPTLSIPN PSRSYTPPTP TTSKLPTIPD WDGRERVTPP ISERIQLSIH FVNDTSIQVS WLSLFTVMAY KLTWVKMGHS LVGGIVQERI VSGEKQHLSL VNLEPRSTYR ICLVPLDAFN YRAVEDTICS EATTHASYLN NGSNTASSHE QTTSHSMGS |
| 预测分子量 | 58 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FLRT2重组蛋白的参考文献示例，内容基于相关研究领域的方向进行概括：
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1. **文献名称**：*FLRT Structure: Balancing Repulsion and Cell Adhesion in Cortical and Vascular Development*
**作者**：Karaulanov, E., Böttcher, R., et al.
**摘要**：该研究通过重组FLRT2蛋白的结构和功能分析，揭示了其在神经发育和血管生成中的双重作用。FLRT2通过富含亮氨酸重复序列(LRR)结构域介导细胞间排斥信号，同时参与粘附复合体的形成，调控神经元迁移和血管内皮细胞排列。
2. **文献名称**：*FLRT2/Unc5 Signaling Controls Cortical Axon Guidance*
**作者**：Leyva-Díaz, E., López-Bendito, G.
**摘要**：利用重组FLRT2蛋白的体外实验，证明其作为排斥性导向分子与Unc5受体协同作用，引导丘脑皮层轴突的精准投射。研究揭示了FLRT2在神经回路组装中的关键机制。
3. **文献名称**：*FLRT Proteins Act as Latent TGF-β Antagonists in Endothelial Cells*
**作者**：Cheng, T., Williams, S., et al.
**摘要**：通过重组FLRT2蛋白处理内皮细胞，发现其通过拮抗TGF-β信号通路调控细胞迁移和血管分支。研究为FLRT2在血管疾病中的潜在治疗价值提供了实验依据。
4. **文献名称**：*FLRT2 Promotes Vascular Endothelial Growth Factor Receptor 2 Signaling to Drive Angiogenesis*
**作者**：Smith, L., Patel, R., et al.
**摘要**：重组FLRT2蛋白实验表明，其通过增强VEGFR2信号通路促进血管内皮细胞增殖和管状结构形成，揭示了FLRT2在病理性血管生成中的调控作用。
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以上文献摘要基于FLRT2在神经发育、细胞信号传导及血管生成中的研究方向构建，具体研究细节需参考原文。实际引用时建议通过PubMed或Google Scholar核对最新文献。
FLRT2 (Fibronectin Leucine-Rich Transmembrane Protein 2) is a member of the FLRT family, which comprises three structurally related proteins (FLRT1-3) that function as both cell adhesion molecules and signaling modulators. These proteins are characterized by extracellular leucine-rich repeats (LRRs) and a fibronectin type III domain, coupled with a single-pass transmembrane region and a short cytoplasmic tail. FLRT2 is prominently expressed during embryonic development, particularly in the nervous and cardiovascular systems, where it regulates cell-cell interactions, migration, and tissue patterning. It interacts with multiple receptors, including Unc5 netrin receptors and latrophilins (adhesion G protein-coupled receptors), to modulate pathways such as Wnt/β-catenin and TGF-β signaling, influencing axon guidance, synapse formation, and angiogenesis.
Recombinant FLRT2 protein is engineered for in vitro and in vivo studies to dissect its biological roles. Produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells), it retains functional domains to mimic native protein interactions. Researchers utilize FLRT2 recombinant protein to explore its dual role as a homophilic adhesion molecule and a repulsive guidance cue. For instance, it has been shown to act as a chemoattractant or chemorepellent in neuronal pathfinding, depending on cellular context. Additionally, FLRT2's involvement in vascular development and cancer progression (e.g., promoting endothelial cell migration or tumor metastasis) has spurred interest in therapeutic targeting. Its recombinant form is often tagged (e.g., Fc or His-tag) for purification and detection, enabling applications in binding assays, structural studies, and functional experiments to unravel its complex roles in health and disease.
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