| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | dltA |
| Uniprot No | P10515 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 93-640aa |
| 氨基酸序列 | KVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLE |
| 预测分子量 | 62.2 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3篇与dltA重组蛋白相关的文献摘要(基于虚拟数据示例)：
1. **《Functional characterization of recombinant DltA protein in Staphylococcus aureus cell wall synthesis》**
- 作者：Smith J, et al.
- 摘要：本研究通过在大肠杆菌中克隆并纯化dltA基因编码的D-丙氨酰载体蛋白连接酶(DltA)，证实其在体外催化D-丙氨酸与载体蛋白的结合，为研究革兰氏阳性菌细胞壁修饰机制提供关键酶学数据。
2. **《Purification and enzymatic analysis of the dltA-encoded enzyme in Bacillus subtilis》**
- 作者：Wang L, et al.
- 摘要：通过构建His标签重组dltA蛋白，优化表达条件并测定其ATP依赖性酶活，揭示了DltA在细菌D-丙氨酸代谢中的磷酸化调控机制。
3. **《Role of recombinant DltA in modulating bacterial resistance to antimicrobial peptides》**
- 作者：García R, et al.
- 摘要：利用重组dltA蛋白进行功能缺失实验，证明其在乳酸杆菌中通过调控细胞壁D-丙氨酸化水平影响阳离子抗菌肽的敏感性，为靶向dlt操纵子的抗感染策略提供依据。
注：以上为模拟示例，实际文献需通过PubMed或Web of Science检索关键词“dltA recombinant protein”获取。
**Background of dltA Recombinant Protein**
The *dltA* gene encodes a critical enzyme involved in the D-alanylation of teichoic acids (TAs), a process essential for modifying the cell envelope of Gram-positive bacteria. This gene is part of the *dlt* operon (*dltA-dltD*), which regulates the incorporation of D-alanine into lipoteichoic acids (LTAs) and wall teichoic acids (WTAs). The DltA protein functions as a D-alanyl carrier protein ligase (ACPS ligase), activating D-alanine via ATP-dependent ligation to a carrier protein (DltC), enabling its transfer to TAs. This modification modulates bacterial surface charge, influencing interactions with host immune components (e.g., cationic antimicrobial peptides) and environmental stressors.
Recombinant DltA protein is produced using heterologous expression systems (e.g., *E. coli*), enabling structural and functional studies. Its production aids in elucidating mechanisms of bacterial virulence, particularly in pathogens like *Staphylococcus aureus* and *Streptococcus pneumoniae*, where D-alanylation enhances resistance to host defenses. Researchers leverage recombinant DltA to explore its enzymatic activity, substrate specificity, and potential as a therapeutic target. Inhibiting DltA could disrupt bacterial membrane integrity, offering strategies to combat antibiotic-resistant infections.
Additionally, recombinant DltA is utilized in structural biology (e.g., crystallography) to map catalytic sites and design inhibitors. Its role in biofilm formation and immune evasion further underscores its relevance in vaccine development and antimicrobial research. By studying this protein, scientists aim to unravel bacterial adaptation mechanisms and develop novel interventions against Gram-positive infections.
In summary, *dltA* recombinant protein serves as a vital tool for understanding bacterial physiology, host-pathogen interactions, and advancing antimicrobial therapies.
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