| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SCPEP1 |
| Uniprot No | Q9HB40-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-452aa |
| 氨基酸序列 | MELALRRSPV PRWLLLLPLL LGLNAGAVID WPTEEGKEVW DYVTVRKDAY MFWWLYYATN SCKNFSELPL VMWLQGGPGG SSTGFGNFEE IGPLDSDLKP RKTTWLQAAS LLFVDNPVGT GFSYVNGSGA YAKDLAMVAS DMMVLLKTFF SCHKEFQTVP FYIFSESYGG KMAAGIGLEL YKAIQRGTIK CNFAGVALGD SWISPVDSVL SWGPYLYSMS LLEDKGLAEV SKVAEQVLNA VNKGLYREAT ELWGKAEMII EQNTDGVNFY NILTKSTPTS TMESSLEFTQ SHLVCLCQRH VRHLQRDALS QLMNGPIRKK LKIIPEDQSW GGQATNVFVN MEEDFMKPVI SIVDELLEAG INVTVYNGQL DLIVDTMGQE AWVRKLKWPE LPKFSQLKWK ALYSDPKSLE TSAFVKSYKN LAFYWILKAG HMVPSDQGDM ALKMMRLVTQ QE |
| 预测分子量 | 49 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SCPEP1重组蛋白的模拟参考文献示例(实际文献可能需要通过学术数据库验证)：
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1. **文献名称**：*Recombinant SCPEP1 Protein Expression and Its Role in Cellular Metabolism*
**作者**：Chen, L. et al.
**摘要**：本研究成功构建了SCPEP1重组蛋白的原核表达系统(大肠杆菌)，并通过亲和层析纯化获得高纯度蛋白。实验表明，SCPEP1具有羧肽酶活性，可特异性水解C端芳香族氨基酸残基，可能在细胞内肽段代谢调控中发挥作用。
2. **文献名称**：*Functional Characterization of SCPEP1 in Lipid Homeostasis Using Recombinant Protein*
**作者**：Kim, S. et al.
**摘要**：通过哺乳动物细胞(HEK293)表达重组SCPEP1蛋白，发现其能够结合并降解脂质代谢相关多肽。动物模型实验显示，SCPEP1缺失导致小鼠肝脏脂质蓄积，提示其在脂质稳态中的潜在调节作用。
3. **文献名称**：*Crystal Structure and Substrate Specificity of Human SCPEP1*
**作者**：Watanabe, T. et al.
**摘要**：解析了重组SCPEP1蛋白的晶体结构(PDB ID: XXXX)，揭示其活性位点与底物结合的关键氨基酸残基。酶动力学分析表明，SCPEP1对含酪氨酸的底物具有最高催化效率，为设计特异性抑制剂奠定基础。
4. **文献名称**：*SCPEP1 Recombinant Protein as a Potential Biomarker in Colorectal Cancer*
**作者**：García, M. et al.
**摘要**：通过ELISA检测发现，结直肠癌患者血清中SCPEP1重组蛋白水平显著升高。体外实验证实，过表达SCPEP1促进癌细胞侵袭，提示其可能作为癌症诊断标志物或治疗靶点。
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**注意**：以上内容为模拟生成，实际文献需通过PubMed、Web of Science等平台检索关键词“SCPEP1 recombinant protein”或“Serine carboxypeptidase 1”获取。若研究较少，可扩展至SCPEP1的同源蛋白或相关代谢通路文献。
SCPEP1 (Serine Carboxypeptidase 1) is a lysosomal enzyme belonging to the serine carboxypeptidase family, which plays a role in protein metabolism by cleaving carboxyl-terminal amino acids from peptides and proteins. It is encoded by the *SCPEP1* gene in humans and is involved in cellular catabolic processes, particularly in lysosomal degradation pathways. The enzyme’s activity is pH-dependent, optimized for the acidic environment of lysosomes, and it contributes to maintaining proteostasis by processing bioactive peptides or regulating protein turnover.
Recombinant SCPEP1 protein is produced using biotechnological methods, typically through heterologous expression in mammalian, insect, or bacterial cell systems. This involves cloning the *SCPEP1* gene into expression vectors, followed by transfection into host cells for protein synthesis. Post-translational modifications, such as glycosylation critical for its stability and enzymatic function, often necessitate eukaryotic expression systems (e.g., HEK293 or CHO cells). The purified recombinant protein retains catalytic activity, enabling researchers to study its biochemical properties, substrate specificity, and interaction with inhibitors.
Research on SCPEP1 has implications for understanding lysosomal storage disorders, neurodegenerative diseases, and metabolic dysregulation. Abnormalities in lysosomal enzymes, including SCPEP1. are linked to conditions like Gaucher disease or Parkinson’s disease. Recombinant SCPEP1 is also utilized in drug discovery to screen for modulators of enzymatic activity or to develop enzyme replacement therapies. Recent studies explore its potential role in processing signaling peptides, suggesting broader regulatory functions beyond degradation. However, its precise physiological substrates and disease associations remain under investigation, highlighting the need for further mechanistic studies using recombinant protein tools.
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