纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | araA |
Uniprot No | P94523 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-496aa |
氨基酸序列 | MLQTKDYEFWFVTGSQHLYGEETLELVDQHAKSICEGLSGISSRYKITHKPVVTSPETIRELLREAEYSETCAGIITWMHTFSPAKMWIEGLSSYQKPLMHLHTQYNRDIPWGTIDMDFMNSNQSAHGDREYGYINSRMGLSRKVIAGYWDDEEVKKEMSQWMDTAAALNESRHIKVARFGDNMRHVAVTDGDKVGAHIQFGWQVDGYGIGDLVEVMDRITDDEVDTLYAEYDRLYVISEETKRDEAKVASIKEQAKIELGLTAFLEQGGYTAFTTSFEVLHGMKQLPGLAVQRLMEKGYGFAGEGDWKTAALVRMMKIMAKGKRTSFMEDYTYHFEPGNEMILGSHMLEVCPTVALDQPKIEVHSLSIGGKEDPARLVFNGISGSAIQASIVDIGGRFRLVLNEVNGQEIEKDMPNLPVARVLWKPEPSLKTAAEAWILAGGAHHTCLSYELTAEQMLDWAEMAGIESVLISRDTTIHKLKHELKWNEALYRLQK |
预测分子量 | 63.6 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araA重组蛋白的3篇示例参考文献(内容为模拟,供参考):
1. **文献名称**: "Cloning and Expression of araA Gene from Escherichia coli for L-Arabinose Isomerase Production"
**作者**: Smith J, et al.
**摘要**: 本研究克隆了大肠杆菌araA基因,并在重组大肠杆菌中高效表达L-阿拉伯糖异构酶。通过优化诱导条件,酶活性提高5倍,为工业生产D-塔格糖奠定了基础。
2. **文献名称**: "Structural Analysis of Recombinant AraA Protein Reveals Substrate Specificity Mechanism"
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析araA重组蛋白的三维结构,发现其活性中心关键氨基酸残基对阿拉伯糖识别的分子机制,为酶工程改造提供理论依据。
3. **文献名称**: "Application of Immobilized AraA in Continuous Production of Rare Sugars"
**作者**: Gupta R, et al.
**摘要**: 将重组araA蛋白固定化并用于生物反应器,实现D-塔格糖的连续合成。优化后转化率达85%,证实其工业化应用的可行性。
*注:以上文献信息为模拟创作,实际研究中建议通过PubMed或Web of Science检索真实文献。*
AraA recombinant protein, commonly referred to as L-arabinose isomerase, is a biocatalytic enzyme with significant industrial and biotechnological relevance. Naturally found in microbial species like *Escherichia coli* and *Bacillus subtilis*, AraA catalyzes the isomerization of L-arabinose to L-ribulose in arabinose metabolism pathways. Its recombinant form is engineered through heterologous expression systems (e.g., *E. coli*, yeast, or *Bacillus* hosts) to enhance production efficiency, stability, or substrate specificity for industrial applications.
The interest in AraA stems from its ability to produce rare sugars, particularly L-ribulose and its derivatives, which serve as low-calorie sweeteners or precursors for pharmaceuticals. For example, L-ribulose can be converted to L-ribose, a key component in antiviral drugs like ribavirin. Recombinant AraA variants are often optimized via protein engineering to operate under non-physiological conditions (e.g., high temperatures or acidic pH) required in industrial processes. Additionally, its role in metabolic engineering for biofuel production—by enabling the utilization of arabinan-rich biomass—has spurred research into its catalytic mechanisms and structural properties.
Studies on AraA recombination typically focus on improving thermostability, catalytic activity, or altering substrate preference through mutagenesis or fusion tags. Advanced techniques like X-ray crystallography and computational modeling are employed to understand its active site architecture and guide rational design. Commercial interest in AraA continues to grow, driven by demand for sustainable enzyme-driven processes in food, pharmaceutical, and bioenergy sectors. Its development exemplifies the intersection of enzymology, synthetic biology, and industrial biotechnology.
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