| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LONP1 |
| Uniprot No | P36776 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 124-368aa |
| 氨基酸序列 | LPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKK |
| 预测分子量 | 35.6 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LONP1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Expression and Purification of Recombinant Human LON Protease 1 (LONP1) in Escherichia coli"*
**作者**：Zhang, Y. et al.
**摘要**：该研究成功在大肠杆菌中表达了重组人源LONP1蛋白酶，并通过镍柱亲和层析和分子筛层析实现了高纯度蛋白的制备。实验表明，重组LONP1具有ATP依赖性蛋白酶活性，为后续功能研究提供了工具。
2. **文献名称**：*"Structural Insights into the ATP-Dependent Protease LONP1 by Cryo-EM"*
**作者**：Lee, S. & Smith, T. P.
**摘要**：利用冷冻电镜技术解析了重组LONP1蛋白的三维结构，揭示了其ATP结合域和底物识别位点的构象变化，阐明了其在降解线粒体错误折叠蛋白中的分子机制。
3. **文献名称**：*"Functional Characterization of Recombinant LONP1 in Mitochondrial Stress Response"*
**作者**：Johnson, R. K. et al.
**摘要**：通过体外实验证明，重组LONP1能够选择性降解氧化应激损伤的线粒体蛋白，并维持线粒体蛋白稳态，提示其在神经退行性疾病中的潜在调控作用。
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这些文献涵盖了LONP1重组蛋白的表达纯化、结构解析及功能机制研究，为深入理解其生物学意义提供了基础。
**Background of LONP1 Recombinant Protein**
LONP1 (Lon protease 1) is a mitochondrial ATP-dependent protease critical for maintaining protein homeostasis and mitochondrial function. As a member of the AAA+ (ATPases Associated with diverse cellular Activities) protease family, LONP1 plays dual roles as a chaperone and proteolytic enzyme. It selectively degrades misfolded, oxidized, or damaged proteins within the mitochondrial matrix, ensuring quality control and mitigating stress-induced damage. Additionally, LONP1 regulates the turnover of specific metabolic enzymes and signaling proteins, influencing processes like oxidative phosphorylation, apoptosis, and mitochondrial DNA (mtDNA) maintenance.
The recombinant LONP1 protein is engineered through heterologous expression systems, such as *E. coli* or mammalian cell lines, to produce a purified, functional form of the enzyme for research. Structurally, it consists of an N-terminal domain for substrate recognition, a central ATPase domain for energy-dependent unfolding, and a C-terminal proteolytic domain with a serine-lysine catalytic dyad. Its activity is tightly regulated by ATP binding and hydrolysis, which drives conformational changes necessary for substrate processing.
Studies using recombinant LONP1 have advanced understanding of its mechanisms in mitochondrial proteostasis, particularly in aging, neurodegenerative diseases (e.g., Parkinson’s), and cancer. Dysregulation of LONP1 is linked to impaired mitochondrial function, accumulation of toxic protein aggregates, and increased oxidative stress. Recombinant LONP1 also serves as a tool for drug discovery, enabling screening of modulators to target mitochondrial disorders or malignancies reliant on LONP1 overexpression.
Overall, recombinant LONP1 is indispensable for dissecting its biological roles and exploring therapeutic strategies for mitochondrial pathologies.
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