| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | dsdA |
| Uniprot No | B4TA53 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-440aa |
| 氨基酸序列 | MENIQKLIARYPLVEDLVALKETTWFNPGATSLAQGLPYVGLTEQDVNAAHDRLARFAPYLAKAFPQTAAAGGMIESDVVAIPAMQKRLEKEYGQTIDGEMLLKKDSHLAISGSIKARGGIYEVLTHAEKLALEAGLLTTDDDYSVLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSACIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEDDYGVAVEQGRKAAQSDPNCFFIDDENSRTLFLGYAVAGQRLKAQFAQQGRVVDASHPLFVYLPCGVGGGPGGVAFGLKLAFGDNVHCFFAEPTHSPCMLLGVYTGLHDAISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGLYTLDDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRICAAAAYQQRHGFSQTQLGNATHLVWATGGGMVPEDEMEQYLAKGR |
| 预测分子量 | 63.3 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dsdA重组蛋白的3篇参考文献概览：
1. **文献名称**: *Cloning and expression of the dsdA gene from Escherichia coli: Characterization of the recombinant D-serine deaminase*
**作者**: Smith, J.R., & Johnson, L.M.
**摘要**: 本研究报道了大肠杆菌dsdA基因的克隆及其在大肠杆菌表达系统中的重组表达。作者纯化了重组D-丝氨酸脱氨酶，并分析了其酶动力学参数，证明其在D-丝氨酸代谢中的高效催化活性。
2. **文献名称**: *Crystal structure of recombinant DsdA protein from Salmonella typhimurium: Insights into substrate specificity*
**作者**: Chen, X., et al.
**摘要**: 通过X射线晶体学解析了沙门氏菌重组DsdA蛋白的三维结构，揭示了其与底物D-丝氨酸结合的活性位点特征，为设计基于该酶的生物传感器提供了结构基础。
3. **文献名称**: *Application of recombinant DsdA as a novel selection marker in synthetic biology*
**作者**: Wang, Y., et al.
**摘要**: 研究利用重组DsdA蛋白的D-丝氨酸降解能力，开发了一种无抗生素的合成生物学筛选系统，验证了其在质粒稳定性维持和基因工程菌株构建中的有效性。
注：以上文献信息为示例性质，实际引用时需核实具体来源及细节。
**Background of DsdA Recombinant Protein**
The *dsdA* gene encodes D-serine deaminase, an enzyme that catalyzes the degradation of D-serine to pyruvate and ammonia. Originally identified in *Escherichia coli*, this enzyme plays a role in bacterial nitrogen metabolism and detoxification, as elevated levels of D-serine can inhibit cell growth. The *dsdA* gene and its protein product have gained attention in molecular biology and synthetic biology due to their utility as a selection marker. Unlike traditional antibiotic resistance genes, DsdA enables plasmid maintenance in bacteria by conferring the ability to metabolize D-serine in growth media, providing an antibiotic-free selection system. This approach aligns with emerging biotechnological trends to minimize antibiotic use, reducing risks of resistance gene spread.
Recombinant DsdA protein is produced via heterologous expression in bacterial hosts, often purified for structural or functional studies. Its enzymatic activity is harnessed in synthetic biology for designing genetic circuits, biosensors, or metabolic engineering applications. For instance, DsdA can serve as a metabolic "switch" in engineered microbes, linking D-serine catabolism to pathway regulation. Additionally, its orthogonality to eukaryotic systems makes it a candidate for conditional control in mammalian cell engineering.
Research also explores DsdA’s role in microbial community dynamics, as D-serine is a signaling molecule in biofilms and host-microbe interactions. Engineering DsdA-expressing strains could modulate these processes for therapeutic or environmental applications. Overall, DsdA exemplifies how fundamental bacterial metabolism insights translate into versatile tools for biotechnology, offering sustainable solutions and novel engineering strategies.
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