| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NEDD4L |
| Uniprot No | Q96PU5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-975aa |
| 氨基酸序列 | ATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGSRTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSAPAGRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKTSLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD |
| 预测分子量 | 138.5 kDa |
| 蛋白标签 | GST 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NEDD4L重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
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1. **标题**：*Structural and functional analysis of recombinant NEDD4L in epithelial sodium channel regulation*
**作者**：Smith A, et al.
**摘要**：本研究通过大肠杆菌系统表达并纯化了人源NEDD4L重组蛋白，解析了其WW结构域与ENaC相互作用的分子机制，证实NEDD4L通过泛素化调控ENaC的细胞膜稳定性。
2. **标题**：*Recombinant NEDD4L ubiquitin ligase activity assay and its role in hypertension*
**作者**：Zhang L, et al.
**摘要**：利用昆虫细胞系统制备高活性NEDD4L重组蛋白，开发了体外泛素化检测体系，发现其活性受磷酸化修饰调控，并验证其在肾小管钠离子代谢异常相关高血压中的作用。
3. **标题**：*Expression optimization and crystallographic study of NEDD4L C2 domain*
**作者**：Tanaka K, et al.
**摘要**：通过哺乳动物表达系统获得NEDD4L的C2结构域重组蛋白，利用X射线晶体学解析其三维结构，揭示了该结构域在膜定位中的钙离子依赖性结合特性。
4. **标题**：*NEDD4L recombinant protein inhibits cancer cell proliferation via PTEN/Akt pathway*
**作者**：Chen H, et al.
**摘要**：在HEK293细胞中表达并纯化NEDD4L重组蛋白，证明其通过增强PTEN稳定性抑制Akt信号通路，显著降低结直肠癌细胞增殖能力。
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建议通过PubMed或Google Scholar搜索真实文献(关键词：NEDD4L recombinant protein, expression, ubiquitination)，注意核对发表年份及期刊权威性。
NEDD4L (Neuronal Precursor Cell-Expressed Developmentally Downregulated 4-Like) is a member of the HECT-type E3 ubiquitin ligase family, known for regulating protein stability and trafficking through ubiquitination. It shares structural homology with other NEDD4 family members, featuring an N-terminal C2 domain (mediating membrane interactions), multiple WW domains (substrate recognition), and a catalytic HECT domain (ubiquitin transfer). NEDD4L primarily targets membrane proteins, including ion channels (e.g., ENaC, NCC) and receptors (e.g., EGFR, TGF-β receptors), modulating their endocytosis or degradation. Its activity is tightly controlled by phosphorylation, particularly via kinases like SGK1 and AMPK, which influence substrate binding or subcellular localization.
Recombinant NEDD4L proteins are engineered to study its enzymatic mechanisms, substrate specificity, and regulatory pathways. These proteins are typically expressed in bacterial or mammalian systems, often with tags (e.g., GST, His) for purification. Researchers use them in *in vitro* ubiquitination assays, structural studies, or high-throughput screens to identify inhibitors/activators. Dysregulation of NEDD4L is linked to hypertension (via ENaC overactivation), cancer (aberrant TGF-β signaling), and neurodevelopmental disorders. Recombinant forms enable exploration of disease-related mutations (e.g., Liddle syndrome variants) and therapeutic targeting. Recent studies also highlight its role in viral infection (e.g., SARS-CoV-2 budding) and autophagy, expanding its biomedical relevance. Despite progress, challenges remain in understanding context-dependent substrate selection and tissue-specific regulation.
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