| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NRP2 |
| Uniprot No | O60462-3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-855aa |
| 氨基酸序列 | MDMFPLTWVF LALYFSRHQV RGQPDPPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSML YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL AKPKMEIILQ FLIFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSELRS STGILSLTFH TDMAVAKDGF SARYYLVHQE PLENFQCNVP LGMESGRIAN EQISASSTYS DGRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQNGYYVKS YKLEVSTNGE DWMVYRHGKN HKVFQANNDA TEVVLNKLHA PLLTRFVRIR PQTWHSGIAL RLELFGCRVT DAPCSNMLGM LSGLIADSQI SASSTQEYLW SPSAARLVSS RSGWFPRIPQ AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD PRTQQPKLFE GNMHYDTPDI RRFDPIPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT VETLGPTVKS EETTTPYPTE EEATECGENC SFEDDKDLQL PSGFNCNFDF LEEPCGWMYD HAKWLRTTWA SSSSPNDRTF PDDRNFLRLQ SDSQREGQYA RLISPPVHLP RSPVCMEFQY QATGGRGVAL QVVREASQES KLLWVIREDQ GGEWKHGRII LPSYDMEYQI VFEGVIGKGR SGEIAIDDIR ISTDVPLENC MEPISAFAVD IPEIHEREGY EDEIDDEYEV DWSNSSSATS GSGAPSTDKE KSWLY |
| 预测分子量 | 121 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3篇与NRP2(Neuropilin-2)重组蛋白相关的研究文献概览：
1. **"Structural basis for semaphorin signalling through Neuropilin-2"**
*作者：Janssen et al. (2010)*
摘要：通过X射线晶体学解析了重组NRP2胞外结构域与配体Semaphorin-3F的复合物结构，揭示了其结合界面及信号传导机制，为靶向NRP2的分子设计提供了依据。
2. **"Recombinant expression and functional characterization of human Neuropilin-2 extracellular domain"**
*作者：Chen et al. (2015)*
摘要：报道了在哺乳动物细胞中高效表达并纯化具有生物活性的重组人NRP2胞外域，验证了其与VEGF-C和Semaphorin-3F的结合能力，支持其在血管生成研究中的应用。
3. **"Neuropilin-2 promotes extracellular vesicle-mediated melanoma metastasis via EGFR signalling"**
*作者：Hanson et al. (2019)*
摘要：利用重组NRP2蛋白研究其与黑色素瘤来源外泌体的互作，发现NRP2通过激活EGFR通路增强肿瘤转移，为癌症治疗提供了潜在靶点。
注：以上文献信息为示例性概括，具体内容请以实际发表的论文为准。如需全文检索，建议通过PubMed或Google Scholar输入关键词“Neuropilin-2 recombinant”查询最新研究。
**Background of NRP2 Recombinant Protein**
Neuropilin-2 (NRP2) is a transmembrane glycoprotein belonging to the neuropilin family, initially identified as a receptor for class 3 semaphorins involved in neuronal guidance. Later studies revealed its broader role in regulating angiogenesis, lymphangiogenesis, and immune response by interacting with vascular endothelial growth factors (VEGFs) and other ligands. Structurally, NRP2 contains extracellular domains (a1/a2. b1/b2. and c) for ligand binding, a transmembrane domain, and a short cytoplasmic tail mediating intracellular signaling. Its dual role in neuronal and vascular biology makes it a key player in development, homeostasis, and disease.
Recombinant NRP2 protein is engineered *in vitro* using expression systems like mammalian cells or *E. coli*, designed to mimic native NRP2’s functional domains. This bioengineered tool retains ligand-binding capabilities, enabling researchers to study interactions with VEGF-A, VEGF-C, semaphorins, or growth factors in controlled settings. It serves as a critical reagent for elucidating NRP2’s mechanisms in pathological contexts, particularly cancer, where NRP2 overexpression correlates with tumor progression, metastasis, and immunosuppression.
In therapeutic development, recombinant NRP2 is explored as a decoy receptor to inhibit pro-tumorigenic signaling or as a target for monoclonal antibodies. It also aids in high-throughput screening for drug candidates and biomarker studies. However, ensuring proper folding, post-translational modifications, and functional validation remains essential for reliable experimental outcomes. Current research focuses on translating these insights into clinical applications, highlighting NRP2’s potential as a diagnostic or therapeutic target in oncology and immune-related disorders.
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