| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | THOP1 |
| Uniprot No | P52888 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-689aa |
| 氨基酸序列 | KPPAACAGDMADAASPCSVVNDLRWDLSAQQIEERTRELIEQTKRVYDQV GTQEFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPSKDIRTASTEA DKKLSEFDVEMSMREDVYQRIVWLQEKVQKDSLRPEAARYLERLIKLGRR NGLHLPRETQENIKRIKKKLSLLCIDFNKNLNEDTTFLPFTLQELGGLPE DFLNSLEKMEDGKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEE NCAILKELVTLRAQKSRLLGFHTHADYVLEMNMAKTSQTVATFLDELAQK LKPLGEQERAVILELKRAECERRGLPFDGRIRAWDMRYYMNQVEETRYCV DQNLLKEYFPVQVVTHGLLGIYQELLGLAFHHEEGASAWHEDVRLYTARD AASGEVVGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQIAIAAMVAN FTKPTADAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFV EAPSQMLENWVWEQEPLLRMSRHYRTGSAVPRELLEKLIESRQANTGLFN LRQIVLAKVDQALHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHL AGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLNSKVGMDYRSCILRPGGS EDASAMLRRFLGRDPKQDAFLLSKGLQVGGCEPEPQVC |
| 预测分子量 | 79 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THOP1重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*"Recombinant human thimet oligopeptidase: expression, purification, and characterization of a novel metallopeptidase"*
**作者**：Dantas, C.F. et al.
**摘要**：该研究在大肠杆菌中成功表达并纯化了重组人源THOP1.证实其具有内切蛋白酶活性，并依赖金属离子催化底物水解，为后续酶学机制研究奠定基础。
2. **文献名称**：*"Structural basis of substrate specificity in thimet oligopeptidase (THOP1) revealed by X-ray crystallography"*
**作者**：Ray, S. et al.
**摘要**：通过重组THOP1蛋白的结晶和结构解析，揭示了其底物结合口袋的构象特征，阐明了其对特定长度多肽的选择性切割机制。
3. **文献名称**：*"THOP1 modulates Aβ peptide degradation and its overexpression exacerbates Alzheimer’s disease pathology in mice"*
**作者**：Tominaga, M. et al.
**摘要**：利用重组THOP1进行体外实验，发现其可剪切淀粉样蛋白Aβ，但在转基因小鼠模型中过量表达反而加速斑块沉积，提示其在阿尔茨海默病中的复杂作用。
注：以上文献信息为基于领域知识的模拟概括，实际引用时建议通过PubMed或Web of Science核对具体文献。
**Background of THOP1 Recombinant Protein**
THOP1 (Thimet Oligopeptidase 1), also known as metalloendopeptidase EC 3.4.24.15. is a zinc-dependent metalloprotease belonging to the M3 family of peptidases. It is ubiquitously expressed in eukaryotic organisms and plays a critical role in intracellular peptide metabolism by cleaving small bioactive peptides (typically 8–17 amino acids). These peptides include neuropeptides, peptide hormones, and antigenic peptides, linking THOP1 to diverse physiological processes such as neuropeptide regulation, antigen presentation, and blood pressure modulation. Its enzymatic activity is calcium-independent but relies on a conserved zinc-binding motif (HEXXH) for catalytic function.
The recombinant THOP1 protein is produced via genetic engineering, often using bacterial (e.g., *E. coli*) or mammalian expression systems. Recombinant expression allows for high-yield production of the enzyme with controlled purity, enabling detailed structural and functional studies. Researchers utilize THOP1 recombinant protein to investigate its substrate specificity, enzymatic kinetics, and interactions with inhibitors or regulatory molecules. Notably, its role in processing peptides like bradykinin, angiotensin, and amyloid-β has sparked interest in neurodegenerative diseases (e.g., Alzheimer’s) and cardiovascular disorders.
Studies also suggest THOP1 involvement in cancer progression, as altered peptidase activity may influence tumor microenvironment signaling. Recombinant THOP1 serves as a tool for drug discovery, particularly in designing inhibitors to modulate peptide-driven pathways. Despite its established roles, mechanisms underlying its substrate selectivity and physiological regulation remain under investigation, highlighting the importance of recombinant protein studies in unraveling THOP1’s biological significance and therapeutic potential.
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