| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | catD |
| Uniprot No | P11504 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-212aa |
| 氨基酸序列 | MVFEKIDKNSWNRKEYFDHYFASVPCTYSMTVKVDITQIKEKGMKLYPAMLYYIAMIVNRHSEFRTAINQDGELGIYDEMIPSYTIFHNDTETFSSLWTECKSDFKSFLADYESDTQRYGNNHRMEGKPNAPENIFNVSMIPWSTFDGFNLNLQKGYDYLIPIFTMGKIIKKDNKIILPLAIQVHHAVCDGFHICRFVNELQELIIVTQVCL |
| 预测分子量 | 32.3 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3篇关于重组组织蛋白酶D(catD)的文献示例(注：文献信息为模拟示例，仅供参考)：
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1. **文献名称**: "Expression and purification of recombinant human cathepsin D in Escherichia coli"
**作者**: Smith J, et al.
**摘要**: 本研究利用大肠杆菌表达系统成功表达了人源重组catD，并通过亲和层析和离子交换层析纯化获得高纯度蛋白。活性分析显示重组catD具有与天然酶相似的蛋白酶活性，为后续功能研究提供了基础。
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2. **文献名称**: "Functional characterization of recombinant cathepsin D in breast cancer cell invasion"
**作者**: Lee S, et al.
**摘要**: 通过哺乳动物细胞(HEK293)表达重组catD，发现其能显著增强乳腺癌细胞的迁移和侵袭能力，并证实其作用依赖于酸性环境下的酶活性，提示catD在肿瘤转移中的潜在机制。
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3. **文献名称**: "Structural insights into recombinant cathepsin D: Implications for Alzheimer's disease therapeutics"
**作者**: García R, et al.
**摘要**: 利用X射线晶体学解析了重组catD的三维结构，发现其与β-淀粉样蛋白前体的结合位点，为开发针对阿尔茨海默病的catD抑制剂提供了结构基础。
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如需真实文献，建议通过PubMed或Google Scholar搜索关键词 **"recombinant cathepsin D"** 获取近期研究。
Cathepsin D (catD) is a lysosomal aspartic protease belonging to the peptidase A1 family, first identified in the 1960s for its role in protein degradation and cellular homeostasis. It is synthesized as an inactive 52 kDa preproenzyme that undergoes proteolytic processing in the lysosome to generate a mature, enzymatically active two-chain form (34 kDa and 14 kDa subunits) linked by disulfide bonds. Structurally, catD features a bilobal architecture typical of aspartic proteases, with a catalytic active site containing two aspartic acid residues critical for substrate cleavage under acidic conditions.
Biologically, catD participates in protein turnover, antigen presentation, and apoptosis regulation. Dysregulation of catD has been linked to neurodegenerative diseases (e.g., Alzheimer's), cancer progression (enhancing tumor invasion and metastasis), and lysosomal storage disorders. This broad pathophysiological relevance drove interest in producing recombinant catD for research and therapeutic applications.
Recombinant catD is typically expressed in mammalian systems (e.g., CHO or HEK293 cells) or yeast to ensure proper post-translational modifications, though Escherichia coli systems are occasionally used for structural studies. The recombinant protein enables detailed mechanistic studies of lysosomal function, drug discovery (e.g., inhibitor screening for cancer therapy), and diagnostic assay development. Recent advances in protein engineering have facilitated the creation of catalytically inactive mutants for substrate-trapping experiments and fluorescently tagged variants for real-time lysosomal activity monitoring. However, challenges persist in maintaining enzyme stability during purification and mimicking the complex lysosomal microenvironment in vitro. Current research focuses on optimizing expression systems and developing targeted delivery mechanisms for potential therapeutic applications.
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