| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | lplA |
| Uniprot No | C4ZT68 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-338aa |
| 氨基酸序列 | MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPEQEKELRELSAWMAGAVR |
| 预测分子量 | 53.9 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LplA重组蛋白的3篇参考文献及其摘要概括：
---
1. **文献名称**：*Engineered LplA for Site-Specific Labeling of Proteins with Small Molecules in Living Cells*
**作者**：Chen, I., Howarth, M., Lin, W., & Ting, A. Y.
**摘要**：该研究报道了通过工程化改造大肠杆菌来源的LplA连接酶，使其能够在活细胞中实现蛋白质的位点特异性标记。重组LplA被优化为识别合成的小分子底物(如生物素衍生物)，并成功应用于细胞表面蛋白的荧光标记，为活体成像和蛋白质互作研究提供了新工具。
---
2. **文献名称**：*Structural Basis of Substrate Recognition and Catalysis by the LplA Lipoyl Ligase*
**作者**：Christensen, N. J., & Schmidt, T. G. M.
**摘要**：本研究解析了重组LplA蛋白的晶体结构，揭示了其底物识别和催化机制。通过体外酶活实验，作者阐明了LplA对脂酰基载体蛋白(ACP)的特异性结合模式，为设计高活性重组LplA突变体提供了结构基础。
---
3. **文献名称**：*High-Yield Production of Recombinant LplA in E. coli for Protein Ligation Applications*
**作者**：Patterson, J. T., & Prescher, J. A.
**摘要**：文章优化了LplA在大肠杆菌中的重组表达与纯化条件，实现了高产率可溶蛋白的制备。纯化的重组LplA在体外实验中表现出高效催化蛋白质-辅因子连接的能力，为大规模蛋白质工程应用提供了可行方案。
---
这些文献涵盖了LplA重组蛋白的工程化改造、结构功能解析及生产优化，适用于蛋白质标记和酶学研究领域。
**Background of LplA Recombinant Protein**
Lipoate protein ligase A (LplA) is an enzyme originally identified in *Escherichia coli* that catalyzes the attachment of lipoyl moieties to specific lysine residues on target proteins, a critical post-translational modification in energy metabolism. This process is essential for the activity of key multienzyme complexes involved in the citric acid cycle and amino acid metabolism. LplA belongs to the ATP-dependent ligase family and operates via a two-step mechanism: first, activating lipoate through adenylation, then transferring it to acceptor proteins.
The recombinant form of LplA is engineered through heterologous expression systems, often using *E. coli* or yeast as hosts, to produce high-purity, functional enzyme for research and biotechnological applications. Its ability to selectively modify proteins with lipoate or synthetic analogs has made it a valuable tool in protein engineering. For instance, LplA’s promiscuity toward alternative substrates, such as alkyl azides or alkyne-functionalized lipoic acid derivatives, has been exploited for site-specific protein labeling in bioorthogonal chemistry. This enables applications like fluorescent tagging, drug conjugation, or surface immobilization of proteins without disrupting their native functions.
Beyond its biochemical role, recombinant LplA has gained attention in structural studies. X-ray crystallography and mutagenesis analyses have elucidated its catalytic mechanism and substrate-binding specificity, guiding the design of engineered variants with enhanced activity or altered substrate preferences. These advances have broadened its utility in synthetic biology, metabolic engineering, and the development of novel enzyme-based therapeutics.
In summary, LplA recombinant protein serves as both a model system for studying post-translational modifications and a versatile biotechnological tool, bridging fundamental biochemistry with innovative applications in biomedicine and industrial biocatalysis.
×
