| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LNX |
| Uniprot No | Q8TBB1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-728aa |
| 活性数据 | MNQPESANDP EPLCAVCGQA HSLEENHFYS YPEEVDDDLI CHICLQALLD PLDTPCGHTY CTLCLTNFLV EKDFCPMDRK PLVLQHCKKS SILVNKLLNK LLVTCPFREH CTQVLQRCDL EHHFQTSCKG ASHYGLTKDR KRRSQDGCPD GCASLTATAP SPEVSAAATI SLMTDEPGLD NPAYVSSAED GQPAISPVDS GRSNRTRARP FERSTIRSRS FKKINRALSV LRRTKSGSAV ANHADQGREN SENTTAPEVF PRLYHLIPDG EITSIKINRV DPSESLSIRL VGGSETPLVH IIIQHIYRDG VIARDGRLLP GDIILKVNGM DISNVPHNYA VRLLRQPCQV LWLTVMREQK FRSRNNGQAP DAYRPRDDSF HVILNKSSPE EQLGIKLVRK VDEPGVFIFN VLDGGVAYRH GQLEENDRVL AINGHDLRYG SPESAAHLIQ ASERRVHLVV SRQVRQRSPD IFQEAGWNSN GSWSPGPGER SNTPKPLHPT ITCHEKVVNI QKDPGESLGM TVAGGASHRE WDLPIYVISV EPGGVISRDG RIKTGDILLN VDGVELTEVS RSEAVALLKR TSSSIVLKAL EVKEYEPQED CSSPAALDSN HNMAPPSDWS PSWVMWLELP RCLYNCKDIV LRRNTAGSLG FCIVGGYEEY NGNKPFFIKS IVEGTPAYND GRIRCGDILL AVNGRSTSGM IHACLARLLK ELKGRITLTI VSWPGTFL |
| 分子量 | 80.6 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人LNX蛋白的模拟参考文献示例(仅供参考，实际文献需查询数据库确认)：
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1. **文献名称**: *"Structural and Functional Analysis of Recombinant Human LNX1 E3 Ubiquitin Ligase"*
**作者**: Nie, J., Chen, D., et al.
**摘要**: 研究报道了重组人LNX1蛋白的表达、纯化及其E3泛素连接酶活性。通过体外泛素化实验，证实LNX1能特异性识别并泛素化底物蛋白NUMB，揭示其在Notch信号通路调控中的作用机制。
2. **文献名称**: *"LNX2 Recombinant Protein Facilitates Neuronal Development via Protein-Protein Interaction Networks"*
**作者**: Suzuki, T., Yamamoto, K., et al.
**摘要**: 利用重组人LNX2蛋白进行免疫共沉淀实验，鉴定其与多种突触蛋白(如Membrin、PDZ结构域蛋白)的相互作用，提示LNX2在神经元分化和突触形成中的关键功能。
3. **文献名称**: *"Recombinant LNX Protein as a Tool for Studying Numb-Mediated Cell Polarity"*
**作者**: McMillan, B. J., Perez-Torrado, R., et al.
**摘要**: 本研究通过表达重组人LNX蛋白，结合细胞模型证明LNX通过泛素化降解NUMB蛋白调控细胞极性，影响干细胞分化和肿瘤细胞迁移过程。
4. **文献名称**: *"Functional Characterization of LNX Protein Domains Using Recombinant Fragments"*
**作者**: Huang, L., Li, W., et al.
**摘要**: 构建重组LNX蛋白不同功能域片段(如RING、PDZ结构域)，系统分析各区域对底物结合和泛素化活性的影响，为开发靶向LNX的小分子抑制剂提供结构基础。
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**注意**：以上文献信息为示例性内容，实际研究中需根据具体LNX亚型(如LNX1/LNX2)及研究方向查阅真实发表的文献。建议通过PubMed或Web of Science以关键词“recombinant LNX”、“LNX ubiquitin ligase”等检索最新进展。
Recombinant human LNX protein refers to a genetically engineered form of Ligand of Numb Protein-X (LNX), a multidomain scaffolding protein involved in cellular signaling and trafficking. LNX belongs to the PDZ (PSD-95/Dlg/ZO-1) domain-containing protein family, known for mediating protein-protein interactions. Human LNX has two paralogs, LNX1 and LNX2. which share structural similarities but exhibit distinct functions. LNX1. the more studied isoform, contains multiple PDZ domains and an N-terminal RING finger domain, enabling its role as an E3 ubiquitin ligase. It interacts with NUMB, a key regulator of Notch signaling, promoting NUMB ubiquitination and degradation to modulate cell differentiation, proliferation, and polarity.
Research on recombinant LNX proteins has advanced understanding of their roles in developmental processes, cancer, and neurological disorders. LNX1's dysregulation is implicated in tumorigenesis, particularly in breast and lung cancers, due to its influence on cell cycle progression and apoptosis. LNX2. though less characterized, is linked to neural development and synaptic function. Recombinant LNX proteins are produced using expression systems like *E. coli* or mammalian cells, enabling *in vitro* studies of protein interactions, post-translational modifications, and pathway analyses. These tools are critical for exploring LNX's therapeutic potential and mechanisms in disease contexts. Their application spans drug discovery, structural biology, and functional genomics, underscoring their importance in both basic and translational biomedical research.
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