| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | speF |
| Uniprot No | P24169 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-732aa |
| 氨基酸序列 | MSKLKIAVSDSCPDCFTTQRECIYINESRNIDVAAIVLSLNDVTCGKLDEIDATGYGIPVFIATENQERVPAEYLPRISGVFENCESRREFYGRQLETAASHYETQLRPPFFRALVDYVNQGNSAFDCPGHQGGEFFRRHPAGNQFVEYFGEALFRADLCNADVAMGDLLIHEGAPCIAQQHAAKVFNADKTYFVLNGTSSSNKVVLNALLTPGDLVLFDRNNHKSNHHGALLQAGATPVYLETARNPYGFIGGIDAHCFEESYLRELIAEVAPQRAKEARPFRLAVIQLGTYDGTIYNARQVVDKIGHLCDYILFDSAWVGYEQFIPMMADCSPLLLDLNENDPGILVTQSVHKQQAGFSQTSQIHKKDSHIKGQQRYVPHKRMNNAFMMHASTSPFYPLFAALNINAKMHEGVSGRNMWMDCVVNGINARKLILDNCQHIRPFVPELVDGKPWQSYETAQIAVDLRFFQFVPGEHWHSFEGYAENQYFVDPCKLLLTTPGIDARNGEYEAFGVPATILANFLRENGVVPEKCDLNSILFLLTPAEDMAKLQQLVALLVRFEKLLESDAPLAEVLPSIYKQHEERYAGYTLRQLCQEMHDLYARHNVKQLQKEMFRKEHFPRVSMNPQEANYAYLRGEVELVRLPDAEGRIAAEGALPYPPGVLCVVPGEIWGGAVLRYFSALEEGINLLPGFAPELQGVYIEEHDGRKQVWCYVIKPRDAQSTLLKGEKL |
| 预测分子量 | 86.4 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. |
以下是假设的3篇关于SpeF重组蛋白的参考文献范例(合理虚构内容供参考)：
1. **《Expression and Characterization of Recombinant SpeF Protein in Escherichia coli》**
- 作者：Smith A. et al. (2020)
- 摘要：研究通过克隆化脓性链球菌的speF基因至大肠杆菌表达系统，成功表达并纯化重组SpeF蛋白，验证其精氨酸脱羧酶活性及在细菌多胺代谢中的作用。
2. **《Functional Analysis of SpeF in Bacterial Stress Response》**
- 作者：Lee J. & Kim S. (2018)
- 摘要：探讨重组SpeF蛋白在应对酸性环境胁迫时的功能，发现其通过调节胞内多胺水平增强细菌存活率，为致病机制研究提供依据。
3. **《Structural Insights into SpeF Enzyme by X-ray Crystallography》**
- 作者：Garcia R. et al. (2021)
- 摘要：利用重组SpeF蛋白进行晶体结构解析，揭示其底物结合域的关键氨基酸残基，为开发靶向抑制剂奠定结构基础。
4. **《Immunogenicity Evaluation of Recombinant SpeF as a Vaccine Candidate》**
- 作者：Chen L. et al. (2019)
- 摘要：评估重组SpeF蛋白在小鼠模型中的免疫保护效果，证实其诱导中和抗体并降低链球菌感染后的组织损伤。
---
注：以上内容为模拟文献，实际研究中请通过学术数据库(如PubMed、Web of Science)以“SpeF”或“ornithine decarboxylase”等关键词检索真实文献。
**Background of speF Recombinant Protein**
SpeF, also known as spermidine acetyltransferase, is a bacterial enzyme encoded by the *speF* gene, primarily studied in *Escherichia coli* and other enteric bacteria. It plays a critical role in polyamine metabolism, a process essential for cellular growth, stress response, and biofilm formation. SpeF catalyzes the acetylation of spermidine, a ubiquitous polyamine, converting it into *N*-acetylspermidine. This reaction regulates intracellular spermidine levels, balancing its beneficial effects (e.g., DNA stabilization) with potential toxicity at high concentrations.
The *speF* gene is part of the polyamine biosynthesis and regulatory network, often induced under stress conditions such as oxidative stress, nutrient limitation, or acidic environments. Dysregulation of SpeF activity can disrupt polyamine homeostasis, impacting bacterial survival, virulence, and adaptability. In pathogenic strains, SpeF has been linked to enhanced tolerance to host defense mechanisms, including antimicrobial peptides, suggesting its role in infection persistence.
Recombinant SpeF protein is produced via heterologous expression systems (e.g., *E. coli* or yeast) for biochemical and structural studies. Its purification enables detailed analysis of enzymatic kinetics, substrate specificity, and inhibitor screening. Research on SpeF also explores its potential as a therapeutic target, particularly in combating antibiotic-resistant infections by disrupting bacterial stress adaptation. Additionally, studies on SpeF contribute to understanding conserved polyamine regulatory mechanisms across species, offering insights into cellular physiology and evolutionary biology.
Overall, SpeF recombinant protein serves as a valuable tool for deciphering polyamine-related pathways and developing strategies to modulate bacterial virulence and resilience.
×
