| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGPEP1 |
| Uniprot No | Q9NXJ5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-209 aa |
| 活性数据 | MEQPRKAVVV TGFGPFGEHT VNASWIAVQE LEKLGLGDSV DLHVYEIPVE YQTVQRLIPA LWEKHSPQLV VHVGVSGMAT TVTLEKCGHN KGYKGLDNCR FCPGSQCCVE DGPESIDSII DMDAVCKRVT TLGLDVSVTI SQDAGRYLCD FTYYTSLYQS HGRSAFVHVP PLGKPYNADQ LGRALRAIIE EMLDLLEQSE GKINYCHKH |
| 分子量 | 23.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下为关于重组人PGPEP1蛋白的3篇代表性文献(注：PGPEP1为假设蛋白名称，实际文献需通过学术数据库验证)：
1. **文献名称**：*"Expression and characterization of recombinant human pyroglutamyl-peptidase I in Escherichia coli"*
**作者**：Smith A et al.
**摘要**：研究利用大肠杆菌系统表达重组人PGPEP1蛋白，优化纯化工艺并验证其酶活性，证明其在生理条件下可高效水解N端焦谷氨酸修饰的多肽。
2. **文献名称**：*"Structural insights into the catalytic mechanism of human PGPEP1 through X-ray crystallography"*
**作者**：Zhang L et al.
**摘要**：通过X射线晶体学解析重组人PGPEP1的三维结构，揭示其催化活性位点及底物结合机制，为靶向药物设计提供结构基础。
3. **文献名称**：*"Functional role of PGPEP1 in regulating oxidative stress via glutathione metabolism"*
**作者**：Kim S et al.
**摘要**：利用重组人PGPEP1蛋白进行细胞实验，发现其通过调控谷胱甘肽代谢通路缓解氧化应激，提示其在神经退行性疾病中的潜在作用。
**注意**：以上为模拟文献，实际研究中建议通过PubMed或Web of Science以“PGPEP1”、“recombinant protein”、“pyroglutamyl aminopeptidase”等关键词检索真实文献。
Recombinant human pyroglutamyl-peptidase I (PGPEP1) protein is a genetically engineered form of the endogenous enzyme involved in regulating bioactive peptides. PGPEP1. also known as pyroglutamyl aminopeptidase, catalyzes the removal of N-terminal pyroglutamate residues from peptides and proteins, a post-translational modification critical for stabilizing peptides against degradation and modulating their biological activity. This enzyme plays roles in various physiological processes, including neurotransmission, hormone regulation, and immune response, by processing peptides like thyrotropin-releasing hormone (TRH) and gonadotropin-releasing hormone (GnRH).
The recombinant version is produced using heterologous expression systems (e.g., E. coli or mammalian cells), enabling high-purity, scalable production for research and therapeutic development. Studies explore its involvement in metabolic disorders, neurodegenerative diseases, and cancer, where aberrant pyroglutamate modification may contribute to pathological conditions. Researchers utilize recombinant PGPEP1 to study substrate specificity, enzymatic mechanisms, and potential therapeutic applications, such as targeting peptide-dependent signaling pathways. Its recombinant form also aids in structural studies, facilitating inhibitor design to modulate enzymatic activity. Despite progress, the full scope of PGPEP1’s biological roles and clinical relevance remains under investigation, highlighting its dual significance in basic biochemistry and applied medical research.
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