首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%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 | LPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTD RAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHE VQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTH TDGIPHLVLSPSTVFFGAFAL |
| 预测分子量 | 19 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LTA(脂磷壁酸)重组蛋白的3篇假设参考文献示例，涵盖其结构、功能及应用研究方向：
---
1. **文献名称**：*Expression and Structural Characterization of Recombinant LTA from Staphylococcus aureus*
**作者**：Zhang Y, et al.
**摘要**：本研究利用大肠杆菌表达系统成功重组表达了金黄色葡萄球菌来源的LTA蛋白，并通过质谱和圆二色谱分析证实其结构与天然LTA高度相似。实验表明重组LTA能够与宿主细胞表面受体TLR2结合，为研究LTA介导的免疫应答机制提供了工具。
2. **文献名称**：*Recombinant LTA as a Novel Antigen for Serodiagnosis of Streptococcal Infections*
**作者**：Wang L, et al.
**摘要**：该研究将重组化脓性链球菌LTA蛋白应用于血清学诊断，开发出基于ELISA的检测方法。临床样本验证显示，重组LTA抗原对链球菌感染的检测灵敏度和特异性分别达92%和88%，表明其在快速诊断中的潜在应用价值。
3. **文献名称**：*Immunomodulatory Effects of Recombinant LTA in Murine Sepsis Models*
**作者**：Chen H, et al.
**摘要**：通过构建小鼠败血症模型，研究发现低剂量重组LTA预处理可显著降低促炎因子(TNF-α、IL-6)水平，并提高生存率。机制研究表明，重组LTA可能通过调控NF-κB信号通路发挥免疫调节作用，为脓毒症治疗提供了新思路。
---
**说明**：以上文献为假设示例，实际研究需查询PubMed、Web of Science等数据库获取真实文献。建议使用关键词"recombinant LTA protein"、"lipoteichoic acid expression"等进行检索。
**Background of LTA Recombinant Protein**
Lymphotoxin-alpha (LTA), also known as tumor necrosis factor-beta (TNF-β), is a cytokine belonging to the TNF superfamily. It plays a critical role in immune regulation, lymphoid organ development, and inflammatory responses. LTA exists in two forms: a membrane-bound heterotrimer (LTA1/LTβ2) and a soluble homotrimer (LTA3). The membrane-bound form, in complex with LTβ, is essential for the formation of secondary lymphoid structures like lymph nodes and Peyer’s patches during development. The soluble form, secreted primarily by activated lymphocytes, binds to TNF receptors (TNFR1/TNFR2) to mediate pro-inflammatory signaling, influencing cell survival, apoptosis, and immune cell recruitment.
Recombinant LTA protein is produced using genetic engineering techniques, often expressed in bacterial, mammalian, or insect cell systems to ensure proper folding and post-translational modifications. Its production enables detailed study of LTA-specific pathways, receptor interactions, and therapeutic applications. Researchers utilize recombinant LTA to investigate its role in autoimmune diseases (e.g., rheumatoid arthritis, multiple sclerosis) and cancers, where dysregulated LTA signaling contributes to pathogenesis.
In drug development, recombinant LTA serves as a tool for screening inhibitors targeting LTA-receptor interactions, offering potential therapies for inflammatory disorders. Additionally, it aids in vaccine research by mimicking immune signals to enhance adaptive responses. Despite structural similarities to TNF-α, LTA’s unique functions in lymphoid neogenesis and immune regulation underscore its distinct therapeutic relevance. Current studies also explore its dual role in promoting or suppressing tumor growth, highlighting context-dependent mechanisms.
Overall, recombinant LTA is vital for unraveling immune biology and advancing targeted treatments for inflammation, autoimmunity, and cancer.
×
