| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APEH |
| Uniprot No | P13798 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-732aa |
| 氨基酸序列 | MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGQYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGPGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDDEIARLKKPDQAIKGDQFVFYEDWGENMVSKSIPVLCVLDVESGNISVLEGVPENVSPGQAFWAPGDAGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLIGGKCELLSDDSLAVSSPRLSPDQCRIVYLQYPSLIPHHQCSQLCLYDWYTKVTSVVVDVVPRQLGENFSGIYCSLLPLGCWSADSQRVVFDSAQRSRQDLFAVDTQVGTVTSLTAGGSGGSWKLLTIDQDLMVAQFSTPSLPPTLKVGFLPSAGKEQSVLWVSLEEAEPIPDIHWGIRVLQPPPEQENVQYAGLDFEAILLQPGSPPDKTQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVEQVLQEEHFDASHVALMGGSHGGFISCHLIGQYPETYRACVARNPVINIASMLGSTDIPDWCVVEAGFPFSSDCLPDLSVWAEMLDKSPIRYIPQVKTPLLLMLGQEDRRVPFKQGMEYYRALKTRNVPVRLLLYPKSTHALSEVEVESDSFMNAVLWLRTHLGS |
| 预测分子量 | 85.2 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APEH重组蛋白的3篇示例参考文献(注：以下内容为模拟示例，实际文献需根据具体研究检索确认)：
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1. **文献名称**: *"Expression and characterization of recombinant human acylpeptide hydrolase"*
**作者**: Smith J, et al.
**摘要**: 本研究报道了在大肠杆菌系统中高效表达并纯化重组人APEH蛋白。通过优化密码子使用和诱导条件，获得了可溶性活性蛋白，并验证了其水解乙酰化短肽的酶活性和底物特异性。
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2. **文献名称**: *"Structural insights into the substrate recognition mechanism of APEH using site-directed mutagenesis"*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析了重组APEH的三维结构，结合定点突变实验，揭示了其底物结合口袋的关键氨基酸残基，阐明了APEH对N端乙酰化肽的选择性催化机制。
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3. **文献名称**: *"Recombinant APEH mitigates amyloid-β toxicity in cellular models of Alzheimer’s disease"*
**作者**: Lee S, et al.
**摘要**: 研究利用HEK293细胞表达重组APEH，发现其能有效降解Aβ40/42淀粉样蛋白，减少神经元细胞毒性，提示APEH在阿尔茨海默病治疗中的潜在应用价值。
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**补充说明**：
- APEH重组蛋白研究多聚焦于**异源表达系统优化**(如大肠杆菌、昆虫细胞)、**酶学特性分析**及**疾病相关功能探索**(如神经退行性疾病、癌症)。
- 实际文献建议通过PubMed/Google Scholar检索关键词“APEH recombinant”或“acylpeptide hydrolase expression”获取最新进展。
如需特定领域文献，可进一步补充研究方向(如蛋白纯化、结构生物学或临床关联)。
APEH (Acylaminoacyl-peptide hydrolase), also known as acylpeptide hydrolase or oxidized protein hydrolase, is a serine protease belonging to the prolyl oligopeptidase family. It plays a critical role in cellular protein quality control by selectively cleaving N-terminally acetylated peptides and degrading oxidatively damaged proteins. This enzyme is ubiquitously expressed in eukaryotes and participates in maintaining proteostasis by removing irreversibly modified proteins that accumulate during oxidative stress or aging.
Recombinant APEH refers to the engineered version of this enzyme produced through heterologous expression systems, typically in E. coli, yeast, or mammalian cells. The development of recombinant APEH technology emerged from the need to study its structure-function relationships, catalytic mechanisms, and potential therapeutic applications. Unlike native APEH isolated from tissues, recombinant forms allow for high-purity production with consistent activity, enabling detailed biochemical characterization and industrial-scale manufacturing.
Structurally, APEH features a characteristic α/β hydrolase fold and a catalytic triad (Ser, Asp, His) common to serine proteases. Its unique substrate specificity for acetylated N-termini distinguishes it from other proteases, making it valuable for protein sequencing applications. Recent studies highlight its potential in neurodegenerative disease research, as it may process amyloid-related peptides, and in cancer biology due to altered expression patterns in tumors.
The recombinant form often incorporates affinity tags (e.g., His-tag) for simplified purification while maintaining native-like activity. Current research focuses on optimizing its stability and catalytic efficiency through protein engineering, exploring its role as a therapeutic target, and developing industrial applications in biotechnology, including peptide synthesis and biocatalysis. Challenges remain in fully understanding its physiological regulation and pathological implications, making recombinant APEH a continued focus of proteomic and drug discovery research.
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