| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pepA |
| Uniprot No | P68768 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-503aa |
| 氨基酸序列 | MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG QGSQNESLMS VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG ATGRPVALLA QFLLNRAGFN GEE |
| 预测分子量 | 54,8 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. |
以下是关于pepA重组蛋白的3篇代表性文献示例(注：文献信息为虚构示例，仅供格式参考)：
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1. **文献名称**: "Cloning, Expression, and Purification of Recombinant pepA from *Escherichia coli*"
**作者**: Zhang et al.
**摘要**: 本研究报道了从大肠杆菌中克隆pepA基因，并在重组表达系统中实现高效可溶性表达。通过优化诱导条件和纯化步骤，获得了高纯度的pepA重组蛋白，并验证了其氨基肽酶活性，为后续功能研究奠定基础。
2. **文献名称**: "Structural Insights into pepA Protease: Crystallographic Analysis of the Recombinant Enzyme"
**作者**: Müller & Schmidt
**摘要**: 利用X射线晶体学解析了重组表达的pepA蛋白的三维结构，揭示了其催化活性中心的关键氨基酸残基及底物结合机制，为开发针对pepA的抑制剂提供了结构基础。
3. **文献名称**: "Biotechnological Application of Recombinant pepA in Peptide Synthesis"
**作者**: Tanaka et al.
**摘要**: 探索了重组pepA在体外肽链合成中的催化潜力，证明其能高效催化特定肽键的形成，在工业酶法合成中具有潜在应用价值。
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如需真实文献，建议通过PubMed或Web of Science检索关键词(如"pepA recombinant protein")，筛选近五年研究以获取最新进展。
**Background of PepA Recombinant Protein**
The PepA (Peptidase A) recombinant protein is a genetically engineered enzyme derived from its native counterpart, commonly found in various prokaryotic and eukaryotic organisms. PepA belongs to the M17 family of metallopeptidases, characterized by their zinc-dependent catalytic activity and involvement in diverse cellular processes, including protein turnover, peptide metabolism, and regulatory functions. In bacteria, PepA often acts as a leucine aminopeptidase, cleaving N-terminal residues from polypeptides, and plays roles in nutrient acquisition, stress response, and virulence regulation. Its homologs in higher organisms are implicated in processes like antigen presentation and neuropeptide processing.
The recombinant form of PepA is typically produced using heterologous expression systems, such as *E. coli* or yeast, to ensure high yield and purity. This engineered protein retains the enzymatic activity and structural integrity of the native enzyme, making it a valuable tool for biochemical and biotechnological applications. Its crystal structure, featuring a conserved hexameric quaternary arrangement and dual zinc-binding motifs, has been extensively studied to elucidate substrate specificity and catalytic mechanisms.
Research on PepA recombinant protein spans multiple fields. In industrial biotechnology, it is explored for peptide synthesis and bioremediation due to its stability and broad substrate range. In medicine, PepA's role in bacterial pathogenesis has spurred interest in developing inhibitors as novel antimicrobial agents. Additionally, its involvement in eukaryotic systems links it to potential therapeutic targets for immune disorders or neurodegenerative diseases. The availability of recombinant PepA facilitates drug discovery, structural studies, and enzyme engineering, underscoring its significance in both basic research and applied sciences.
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