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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LTA |
| Uniprot No | P01374 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-205aa |
| 氨基酸序列 | LPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL |
| 预测分子量 | 20.8 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. |
以下为关于LTA(脂磷壁酸)重组蛋白的3篇模拟参考文献及摘要概括，供参考：
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1. **标题**：*Recombinant Lipoteichoic Acid Protein Expression in E. coli and Its Immunogenicity Analysis*
**作者**：Smith J, et al.
**摘要**：研究利用大肠杆菌系统表达重组LTA蛋白，通过纯化获得高纯度产物，并证实其能激活巨噬细胞释放促炎因子，为革兰氏阳性菌疫苗开发提供候选抗原。
2. **标题**：*Structural and Functional Characterization of a Novel LTA-Binding Protein in Staphylococcus aureus*
**作者**：Wang L, et al.
**摘要**：解析金黄色葡萄球菌LTA结合蛋白的晶体结构，发现其通过特异性识别LTA介导细菌黏附宿主细胞，为抗感染药物靶点设计提供理论依据。
3. **标题**：*LTA-Derived Peptide Conjugate Vaccine Enhances Antibody Responses in Murine Models*
**作者**：Garcia R, et al.
**摘要**：设计基于LTA表位的重组蛋白疫苗，动物实验显示其诱导高水平中和抗体，显著降低小鼠败血症模型中细菌载量，证明其作为预防性疫苗的潜力。
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注：以上文献为示例性质，实际研究需通过PubMed/Google Scholar等平台检索关键词(如"recombinant LTA protein" "lipoteichoic acid vaccine")获取。
**Background of Recombinant LTA (Leukotoxin A) Protein**
Leukotoxin A (LTA), a pore-forming cytotoxin, is primarily produced by *Aggregatibacter actinomycetemcomitans*, a Gram-negative bacterium associated with aggressive periodontitis and systemic inflammatory conditions. LTA belongs to the repeats-in-toxin (RTX) family, characterized by calcium-binding glycine- and aspartate-rich repeats. It exhibits species-specific cytotoxicity, preferentially targeting immune cells like neutrophils and macrophages by binding to β2 integrins (e.g., LFA-1), leading to pore formation, cell activation, or apoptosis.
Recombinant LTA proteins are engineered using genetic cloning techniques, where the *ltxA* gene is expressed in heterologous systems like *E. coli* or mammalian cells. This allows large-scale production of purified LTA for research and therapeutic applications. Recombinant LTA retains structural and functional properties of native toxin, enabling studies on host-pathogen interactions, immune evasion mechanisms, and LTA’s role in inflammatory cascades. It also aids in developing inhibitors, vaccines, or antibody-based therapies targeting LTA-mediated pathologies.
Research highlights LTA’s dual role: while high concentrations cause rapid cell lysis, sublytic doses modulate immune responses, contributing to chronic inflammation. Recombinant LTA tools have clarified its molecular mechanisms, including interactions with lipid rafts and intracellular signaling pathways. Additionally, recombinant variants with mutations (e.g., in catalytic domains) are used to dissect structure-function relationships.
Overall, recombinant LTA proteins are pivotal in advancing understanding of periodontal diseases, systemic inflammation, and bacterial virulence, offering potential for novel diagnostics and therapeutics.
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