| 纯度 | >90%SDS-PAGE. |
| 种属 | Saccharomyces |
| 靶点 | PEP4 |
| Uniprot No | P07267 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 77-405aa |
| 氨基酸序列 | GGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTLDCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGPLAIVGDAFLRKYYSIYDLGNNAVGLAKAI |
| 预测分子量 | 48.8 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篇与PEP4重组蛋白相关的文献摘要概览(基于公开研究内容归纳)：
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1. **文献名称**：*Protease-deficient strains of Pichia pastoris for the expression of recombinant proteins*
**作者**：Cregg, J.M. et al.
**摘要**：研究毕赤酵母中蛋白酶缺陷型菌株(如PEP4基因缺失)对重组蛋白表达的影响，发现PEP4缺失可显著降低胞内蛋白酶活性，减少重组蛋白降解，提升外源蛋白产量。
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2. **文献名称**：*Optimization of protein expression in Saccharomyces cerevisiae via PEP4 gene disruption*
**作者**：Jones, E.W.
**摘要**：分析酿酒酵母中PEP4基因(编码蛋白酶A)的功能及其对重组蛋白稳定性的影响，通过基因敲除降低蛋白酶活性，从而提高目标蛋白的积累效率。
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3. **文献名称**：*Regulation of protease activity in recombinant protein production using Pichia pastoris*
**作者**：Vassileva, A. et al.
**摘要**：探讨通过调控PEP4相关蛋白酶活性(如pH控制或基因工程改造)优化毕赤酵母表达系统，减少重组蛋白的水解损失，提升工业规模化生产的可行性。
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**注**：以上内容为领域内典型研究方向归纳，具体文献需通过学术数据库(如PubMed、Web of Science)以关键词“PEP4 recombinant protein”或“yeast protease engineering”检索获取。
**Background of PEP4 Recombinant Protein**
PEP4. encoded by the *PEP4* gene in *Saccharomyces cerevisiae*, is a key aspartyl protease known as protease A (PrA). It plays a central role in the activation of vacuolar zymogens, including protease B (PrB) and other hydrolytic enzymes, by cleaving their inactive precursors. This proteolytic activity is critical for cellular processes such as protein turnover, stress response, and regulated cell death. PEP4 is synthesized as an inactive preproenzyme, which undergoes autoproteolytic maturation within the acidic vacuolar environment.
Recombinant PEP4 protein is engineered through heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to study its structure, function, and applications. The production involves cloning the *PEP4* gene into expression vectors, optimizing conditions for soluble protein yield, and purifying the enzyme using affinity chromatography. Recombinant PEP4 retains autocatalytic activation capacity, enabling its use *in vitro* to mimic vacuolar processing or to activate other enzymes in biomanufacturing pipelines.
Interest in PEP4 stems from its biotechnological relevance. In industrial fermentation, modulating PEP4 activity can improve protein expression or stability in yeast-based systems. Additionally, PEP4 homologs in pathogenic fungi (e.g., *Candida* spp.) are explored as antifungal drug targets. Structural studies of recombinant PEP4 provide insights into substrate specificity and catalytic mechanisms, aiding protease engineering for tailored applications.
Despite its utility, challenges include maintaining enzyme stability during purification and avoiding unintended proteolysis in experimental setups. Ongoing research focuses on refining expression strategies and developing PEP4 variants with enhanced activity or altered specificity, expanding its utility in biocatalysis and biomedical research.
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