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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFb |
| 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TNF-β(淋巴毒素-α)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：Cloning and expression of human lymphotoxin, a lymphokine with tumour necrosis activity
**作者**：Gray, P.W., Aggarwal, B.B., Benton, C.V. 等
**摘要**：该研究首次克隆了人TNF-β(淋巴毒素)的cDNA，并在大肠杆菌中成功表达重组蛋白，证实其具有体外抗肿瘤活性，为后续功能研究奠定基础(发表于 *Nature*, 1984)。
2. **文献名称**：The structure of tumor necrosis factor-beta at 2.6-A resolution
**作者**：Eck, M.J., Sprang, S.R.
**摘要**：通过X射线晶体学解析TNF-β的三维结构，揭示其与TNF-α的相似性与受体结合差异，为靶向药物设计提供结构依据(发表于 *Journal of Biological Chemistry*, 1989)。
3. **文献名称**：Lymphotoxin-beta receptor signaling is required for the homeostatic control of HEV differentiation and function
**作者**：Browning, J.L., Sizing, I.D., Lawton, P. 等
**摘要**：利用重组TNF-β蛋白研究其在淋巴器官高内皮静脉(HEV)发育中的作用，证实其通过特定受体调控免疫细胞迁移(发表于 *Immunity*, 2005)。
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注：TNF-β通常指淋巴毒素-α(LT-α)，需注意与TNF-α区分。上述研究涵盖早期克隆、结构解析及生理功能，均为该领域里程碑式工作。
Tumor necrosis factor beta (TNF-β), also known as lymphotoxin-alpha (LT-α), is a cytokine belonging to the TNF superfamily. It shares structural homology with TNF-α (~30% amino acid sequence identity) but differs in cellular sources and receptor interactions. TNF-β is primarily produced by activated lymphocytes, including T cells and B cells, and plays a critical role in immune regulation, lymphoid organ development, and inflammatory responses.
As a transmembrane protein, TNF-β can be cleaved to release a soluble homotrimeric form that binds to TNF receptors (TNFR1/TNFR2) and herpesvirus entry mediator (HVEM). Its signaling activates pathways such as NF-κB and MAPK, modulating cell survival, apoptosis, and inflammation. Notably, TNF-β synergizes with TNF-α in promoting cytotoxic effects on tumor cells and regulating adaptive immunity. However, dysregulated TNF-β expression is implicated in autoimmune diseases (e.g., rheumatoid arthritis) and chronic inflammation.
Recombinant TNF-β proteins are typically produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper folding and post-translational modifications. Purification involves affinity chromatography and ion-exchange methods. Quality control includes SDS-PAGE, Western blot, and functional assays (e.g., cytotoxicity tests on TNF-sensitive cell lines like L929).
In research, recombinant TNF-β serves as a tool to study lymphoid neogenesis, immune cell crosstalk, and TNF receptor signaling dynamics. Therapeutic applications focus on neutralizing TNF-β activity in autoimmune disorders or leveraging its pro-inflammatory properties in cancer immunotherapy. Challenges persist in managing its pleiotropic effects, as systemic inhibition or overexpression may lead to off-target immune modulation. Recent studies also explore its role in infectious disease responses and tertiary lymphoid structure formation, highlighting its multifaceted biological significance.
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