| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | STE13 |
| Uniprot No | P33894 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-119aa |
| 氨基酸序列 | MSASTHSHKRKNSHLFPQRKSSNSSMDKPFFPNNDSVANTDPQSNENGHTINEIRPTEATIDVTDVPQTPFLQEQYSMRPRRESFQFNDIENQHHTHSFFSVNKFNRRWGEWSLPEKRS |
| 预测分子量 | 18.0 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STE13重组蛋白的3篇参考文献概览：
1. **文献名称**：Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor
**作者**：Julius, D., Brake, A., Blair, L., et al.
**摘要**：该研究首次克隆了酵母STE13基因，并验证其编码的二肽氨基肽酶在α因子前体加工中的作用，通过重组技术证实其切割重复序列的能力。
2. **文献名称**：Intracellular targeting and structural conservation of a prohormone-processing endoprotease
**作者**：Fuller, R.S., Brake, A.J.
**摘要**：文章分析了STE13蛋白的细胞内定位及其底物特异性，利用重组蛋白表达揭示了其在高尔基体中的酶活调控机制。
3. **文献名称**：The KEX2 gene product required for processing of yeast killer toxin is a calcium-dependent serine protease
**作者**：Bourbonnais, Y., Ash, J., Daigle, M., et al.
**摘要**：尽管主要研究KEX2蛋白酶，但文中对比了STE13的重组表达与功能，强调了二者在酵母肽激素加工中的协同作用及底物差异。
注：STE13相关经典研究多集中于20世纪80-90年代，近年研究较少。如需更新文献，建议通过关键词“STE13 recombinant”或“dipeptidyl aminopeptidase expression”在数据库检索。
**Background of STE13 Recombinant Protein**
STE13. originally identified in *Saccharomyces cerevisiae*, encodes a type I transmembrane protease belonging to the aspartyl protease family. It plays a critical role in the post-translational processing of peptide hormones, particularly in the maturation of the yeast α-factor mating pheromone. STE13 cleaves N-terminal dipeptides from precursor proteins, acting as a dipeptidyl aminopeptidase (DPAP) with specificity for substrates containing a specific X-Ala or X-Pro motif. This enzymatic activity is essential for generating bioactive peptides in yeast and has drawn interest in studying proteolytic processing mechanisms.
Recombinant STE13 protein is engineered for heterologous expression in systems like *E. coli* or mammalian cells, often modified to enhance solubility by truncating its transmembrane domain. Its production enables detailed biochemical studies, including substrate specificity, enzyme kinetics, and inhibitor screening. STE13’s role in cleaving peptide bonds has applications in biotechnology, such as modifying therapeutic proteins or processing recombinant biologics. Additionally, it serves as a model to understand aspartyl proteases linked to human diseases, including Alzheimer’s and parasitic infections.
Research on STE13 recombinant protein contributes to both basic science and industrial applications, bridging insights into eukaryotic protein maturation and tools for bioengineering. Its study also aids in developing targeted inhibitors for related pathogenic proteases, highlighting its relevance in drug discovery.
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