| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CTSL |
| Uniprot No | P07711 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-333aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSTLTFDHS LEAQWTKWKA MHNRLYGMNE EGWRRAVWEK NMKMIELHNQ EYREGKHSFT MAMNAFGDMT SEEFRQVMNG FQNRKPRKGK VFQEPLFYEA PRSVDWREKG YVTPVKNQGQ CGSCWAFSAT GALEGQMFRK TGRLISLSEQ NLVDCSGPQG NEGCNGGLMD YAFQYVQDNG GLDSEESYPY EATEESCKYN PKYSVANDTG FVDIPKQEKA LMKAVATVGP ISVAIDAGHE SFLFYKEGIY FEPDCSSEDM DHGVLVVGYG FESTESDNNK YWLVKNSWGE EWGMGGYVKM AKDRRNHCGI ASAASYPTV |
| 预测分子量 | 38 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. |
1. **"Recombinant human cathepsin L is a functional endoprotease active in acidic conditions"**
- *Authors: Kirschke H, Barrett AJ*
- 摘要：该研究在大肠杆菌中重组表达了人源组织蛋白酶L(CTSL)，验证了其在酸性pH下的蛋白水解活性，并探讨了酶原激活机制及底物特异性。
2. **"Expression and characterization of recombinant cathepsin L in Pichia pastoris"**
- *Authors: Wang F, et al.*
- 摘要：通过毕赤酵母系统高效表达重组CTSL，优化纯化工艺后获得高活性蛋白，分析了其在肿瘤细胞侵袭中的潜在作用及抑制剂筛选应用。
3. **"Crystal structure of human procathepsin L: Insights into its activation and drug design"**
- *Authors: Guncar G, et al.*
- 摘要：解析了重组人CTSL酶原的晶体结构，揭示了其自激活的分子机制，为基于结构的抗转移或抗病毒药物开发提供理论依据。
4. **"Cathepsin L as a target for COVID-19 drug discovery"**
- *Authors: Fonović M, Turk B*
- 摘要：探讨重组CTSL在新冠病毒刺突蛋白切割中的作用，提出其作为抗病毒药物靶点的潜力，并评估了选择性抑制剂的体外效果。
(注：以上为模拟文献，实际引用需根据具体研究通过PubMed等数据库检索。)
Cathepsin L (CTSL), a member of the papain-like cysteine protease family, is a lysosomal enzyme critical for intracellular protein degradation, extracellular matrix (ECM) remodeling, and antigen processing. It is synthesized as an inactive proenzyme (pro-CTSL) that undergoes proteolytic cleavage in acidic lysosomal environments to become enzymatically active. Beyond lysosomal functions, CTSL is implicated in pathological processes such as cancer metastasis, viral entry (e.g., SARS-CoV-2), and neurodegenerative disorders like Alzheimer’s disease.
Recombinant CTSL proteins are engineered using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to produce purified, bioactive forms for research and therapeutic applications. Mammalian systems, such as HEK293 or CHO cells, are often preferred to ensure proper post-translational modifications, including glycosylation, which affects stability and activity. The recombinant protein typically retains the propeptide region for controlled activation and may include affinity tags (e.g., His-tag) for simplified purification.
CTSL’s role in disease pathways has driven interest in its recombinant form for drug discovery. Inhibitors targeting CTSL are explored for anticancer therapies and antiviral agents, while its proteolytic activity is harnessed in vitro for protein processing studies. Additionally, recombinant CTSL serves as a tool to study enzyme-substrate interactions, lysosomal storage disorders, and immune response modulation. Challenges remain in optimizing catalytic efficiency, avoiding off-target effects, and improving delivery systems for therapeutic applications. Ongoing research focuses on structure-function relationships and engineering variants with enhanced specificity or pH-dependent activity to expand biomedical utility.
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