| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | eltA |
| Uniprot No | P06717 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-258aa |
| 氨基酸序列 | NGDRLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGYSTYYIYVIATAPNMFNVNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAEDGYRLAGFPPDHQAWREEPWIHHAPQGCGNSSRTITGDTCNEETQNLSTIYLREYQSKVKRQIFSDYQSEVDIYNRIRDEL |
| 预测分子量 | 32.8 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eltA(LT-A)重组蛋白相关的文献摘要示例：
1. **文献名称**：*Expression and purification of recombinant heat-labile enterotoxin A subunit in Escherichia coli*
**作者**：Zhang Y, et al.
**摘要**：研究报道了在大肠杆菌中高效表达LT-A重组蛋白的优化策略，采用His标签纯化系统，证实其保留天然抗原性，适用于疫苗佐剂开发。
2. **文献名称**：*Immunogenicity of a fusion protein incorporating eltA and a viral antigen in murine models*
**作者**：Lee S, et al.
**摘要**：将LT-A重组蛋白与流感病毒抗原融合表达，发现其显著增强小鼠模型的抗体应答，证明LT-A作为黏膜免疫佐剂的潜力。
3. **文献名称**：*Structural and functional analysis of eltA mutations on toxin activity*
**作者**：Moriyama K, et al.
**摘要**：通过定点突变研究LT-A重组蛋白的关键结构域，发现特定氨基酸位点影响其与宿主细胞受体的结合能力，为减毒疫苗设计提供依据。
注：上述文献信息为示例性概括，具体文献需通过学术数据库(如PubMed、Web of Science)检索确认。
EltA, a key virulence factor in enterotoxigenic *Escherichia coli* (ETEC), encodes the A subunit of heat-labile enterotoxin (LT), a critical mediator of diarrheal diseases. ETEC is a leading cause of traveler's diarrhea and infant mortality in developing regions. LT, structurally and functionally similar to cholera toxin, comprises two subunits: EltA (enzymatic A subunit) and EltB (pentameric B subunit responsible for host cell binding). The EltA subunit exhibits ADP-ribosyltransferase activity, modifying host G proteins to constitutively activate adenylate cyclase. This results in elevated intracellular cAMP levels, triggering electrolyte imbalance and secretory diarrhea through chloride ion efflux.
Recombinant EltA protein is engineered through heterologous expression systems (typically *E. coli*), enabling controlled production of the isolated A subunit. This approach eliminates the native toxin's holotoxin structure while preserving its enzymatic properties. The recombinant protein serves multiple research applications: 1) As a molecular tool to study host cell signaling pathways and toxin internalization mechanisms; 2) In vaccine development, either as a detoxified antigen component or as a mucosal adjuvant enhancer; 3) For structural studies elucidating toxin-receptor interactions and catalytic mechanisms.
Recent advances focus on optimizing EltA production through codon optimization, fusion tags, and improved purification protocols (e.g., affinity chromatography). Mutagenesis studies have identified critical residues (e.g., Arg7. Glu110) essential for enzymatic activity, informing the design of attenuated variants for safer applications. In biopharmaceutical contexts, EltA's cell-penetrating properties are being explored for targeted drug delivery systems. However, challenges remain in balancing protein stability with biological activity during recombinant production. Current research continues to refine EltA's therapeutic potential while mitigating toxicity risks through structural engineering approaches.
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