| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LTbR |
| Uniprot No | P36941 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-227aa |
| 氨基酸序列 | QAVPPYASENQTCRDQEKEYYEPQHRICCSRCPPGTYVSAKCSRIRDTVC ATCAENSYNEHWNYLTICQLCRPCDPVMGLEEIAPCTSKRKTQCRCQPGM FCAAWALECTHCELLSDCPPGTEAELKDEVGKGNNHCVPCKAGHFQNTSS PSARCQPHTRCENQGLVEAAPGTAQSDTTCKNPLEPLPPEMSGTMLMVDH HHHHH |
| 预测分子量 | 23 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条关于LTbR(淋巴毒素β受体)重组蛋白的典型研究方向及文献摘要概括，供参考：
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1. **文献名称**：*Structural insights into ligand recognition by the lymphotoxin-beta receptor*
**作者**：Smith A, et al.
**摘要**：通过X射线晶体学解析LTbR胞外区重组蛋白与配体淋巴毒素α1β2的复合物结构，揭示了受体与配体结合的关键位点，为靶向药物设计提供结构基础。
2. **文献名称**：*Recombinant LTβR-Fc fusion protein attenuates inflammation in autoimmune encephalomyelitis*
**作者**：Chen L, et al.
**摘要**：研究LTbR-Fc重组融合蛋白在实验性自身免疫性脑脊髓炎模型中的作用，证明其通过阻断LTβR信号通路抑制炎症反应和神经损伤。
3. **文献名称**：*Expression and functional characterization of soluble LTβR in modulating NF-κB signaling*
**作者**：Wang Y, et al.
**摘要**：利用哺乳动物细胞系统表达可溶性LTbR重组蛋白，发现其通过竞争性结合配体抑制NF-κB通路活化，提示其在炎症性疾病中的治疗潜力。
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**说明**：以上文献为示例性概括，实际文献需通过PubMed、Web of Science等平台检索关键词(如“LTbR recombinant protein”、“lymphotoxin-beta receptor”)获取。若需具体文献，建议结合研究场景补充关键词(如“结构”、“治疗应用”或“信号机制”)。
Lymphotoxin-beta receptor (LTβR), a member of the tumor necrosis factor receptor superfamily (TNFRSF), is a transmembrane protein critical for immune system regulation and lymphoid tissue development. It binds to its primary ligand, the membrane-bound lymphotoxin-alpha1/beta2 (LTα1β2) heterotrimer, initiating signaling cascades that mediate immune cell communication, lymphoid organogenesis, and inflammatory responses. LTβR is expressed on stromal, epithelial, and myeloid cells, playing a key role in maintaining lymphoid architecture and regulating chemokine production for immune cell trafficking.
Recombinant LTβR proteins, typically engineered as soluble decoy receptors or agonist/antagonist variants, are generated using expression systems like mammalian cells (e.g., HEK293) or bacteria. These proteins retain the extracellular ligand-binding domain to either block LTα1β2 signaling or modulate receptor activation. Research highlights their therapeutic potential in autoimmune diseases (e.g., rheumatoid arthritis, inflammatory bowel disease) and cancer. By disrupting LTβR-mediated pro-inflammatory pathways or impairing tumor-associated lymphoid structures, recombinant LTβR agents have shown efficacy in preclinical models.
Recent studies also explore LTβR's role in chronic inflammation and tertiary lymphoid structure formation in tumors. Clinical trials targeting this pathway, though limited, suggest its relevance in modulating pathological immune responses. Challenges include optimizing receptor-ligand specificity and minimizing off-target effects, but advances in protein engineering continue to refine these therapeutic tools. LTβR remains a compelling target for immune modulation, bridging innate and adaptive immunity through its unique positioning in TNF receptor biology.
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