纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NPEPPS |
Uniprot No | P55786 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 53-504aa |
氨基酸序列 | RLPADVSPINYSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSKYTTPSGEVRYAAVTQFEATDARRAFPCWDEPAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKFARTPVMSTYLVAFVVGEYDFVETRSKDGVCVRVYTPVGKAEQGKFALEVAAKTLPFYKDYFNVPYPLPKIDLIAIADFAAGAMENWGLVTYRETALLIDPKNSCSSSRQWVALVVGHELAHQWFGNLVTMEWWTHLWLNEGFASWIEYLCVDHCFPEYDIWTQFVSADYTRAQELDALDNSHPIEVSVGHPSEVDEIFDAISYSKGASVIRMLHDYIGDKDFKKGMNMYLTKFQQKNAATEDLWESLENASGKPIAAVMNTWTKQMGFP |
预测分子量 | 57.0 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NPEPPS重组蛋白的3篇代表性文献的简要信息:
1. **文献名称**:*Recombinant NPEPPS regulates tau degradation through proteasome activation in cellular models of neurodegeneration*
**作者**:Wang, Y., et al.
**摘要**:本研究利用重组NPEPPS蛋白,证明其通过激活蛋白酶体途径促进异常tau蛋白的降解,为阿尔茨海默病的治疗提供了潜在靶点。
2. **文献名称**:*Structural and functional characterization of human puromycin-sensitive aminopeptidase (NPEPPS) expressed in E. coli*
**作者**:Karstaen, S., et al.
**摘要**:作者通过大肠杆菌系统成功表达并纯化重组NPEPPS蛋白,解析其晶体结构,并揭示其底物结合域的关键氨基酸残基,为酶活性机制研究奠定基础。
3. **文献名称**:*High-throughput screening of NPEPPS inhibitors using recombinant protein-based fluorescence assay*
**作者**:Li, H., et al.
**摘要**:开发基于重组NPEPPS蛋白的荧光检测方法,用于高通量筛选其小分子抑制剂,发现多个候选化合物可调节其氨基肽酶活性,具有药物开发潜力。
*注:以上文献信息为示例性质,实际文献需通过学术数据库检索确认。*
NPEPPS (aminopeptidase P lysosomal, also known as X-Pro aminopeptidase or APPEP) is a metalloenzyme belonging to the peptidase M24B family. It catalyzes the cleavage of N-terminal amino acids from peptides, particularly those with a proline residue in the penultimate position (Xaa-Pro bonds). This enzymatic activity plays a critical role in regulating bioactive peptides, including hormones, neuropeptides, and inflammatory mediators, influencing cellular processes such as protein turnover, peptide signaling, and immune response modulation.
Recombinant NPEPPS protein is engineered using expression systems like *E. coli* or mammalian cells to ensure proper folding and post-translational modifications. Its production enables detailed biochemical studies, including substrate specificity, enzymatic kinetics, and inhibitor screening. Researchers utilize recombinant NPEPPS to explore its involvement in diseases, notably neurodegenerative disorders. For instance, NPEPPS has been implicated in degrading pathological tau proteins in Alzheimer’s disease, with studies suggesting its upregulation may mitigate tau aggregation.
Additionally, NPEPPS interacts with viral proteins and has been studied in HIV pathogenesis, where it modulates viral infectivity. Its role in cancer is emerging, with potential links to metastasis and drug resistance through extracellular matrix remodeling. The recombinant protein also serves as a tool for structural biology, aiding in crystallography and drug design. By providing a purified, active form of the enzyme, recombinant NPEPPS accelerates both basic research and therapeutic development, bridging gaps between cellular function understanding and clinical applications.
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