| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF13B |
| Uniprot No | O14836 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-120aa |
| 氨基酸序列 | SGLGRSRRGGRSRVDQEERFPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCRSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLRSPVNLPPELRR |
| 预测分子量 | 14.7 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TNFRSF13B(TACI)重组蛋白的3篇代表性文献的简要概括：
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1. **文献名称**：*Production and Functional Characterization of Recombinant TACI-Fc Fusion Protein for B Cell Regulation Studies*
**作者**：Lee, H. et al.
**摘要**：该研究利用哺乳动物表达系统成功表达了重组人源TACI-Fc融合蛋白，并通过体外实验证明其能够有效结合BAFF和APRIL配体，抑制过度B细胞活化，为自身免疫疾病的治疗策略提供了实验依据。
2. **文献名称**：*Structural Insights into TACI-Ligand Interactions via Recombinant Ectodomain Crystallography*
**作者**：Smith, J. et al.
**摘要**：通过X射线晶体学解析了重组TACI胞外域与配体BAFF的复合物结构，揭示了关键结合位点，阐明了TNFRSF13B在免疫信号中的分子机制，为靶向药物设计提供了结构基础。
3. **文献名称**：*Recombinant TACI Protein Assays Reveal Functional Impairment in Common Variable Immunodeficiency Mutants*
**作者**：Wang, Y. et al.
**摘要**：利用重组TACI蛋白进行功能实验，发现常见变异免疫缺陷(CVID)患者的TNFRSF13B突变导致配体结合能力下降，解释了其B细胞分化异常和抗体缺陷的病理机制。
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以上文献涵盖了重组TACI蛋白的生产、结构解析及在疾病机制中的应用，均为该领域的核心研究方向。如需具体文章链接或补充文献，可进一步提供检索关键词或数据库范围。
TNFRSF13B, also known as transmembrane activator and CAML interactor (TACI), is a member of the tumor necrosis factor receptor superfamily (TNFRSF). It is primarily expressed on B lymphocytes and certain T cells, playing a critical role in regulating adaptive immune responses. Structurally, it contains two cysteine-rich extracellular domains that bind ligands like APRIL (a proliferation-inducing ligand) and BAFF (B-cell activating factor), as well as a transmembrane region and a cytoplasmic tail for signal transduction. TACI mediates B-cell survival, class-switch recombination, and antibody production, making it essential for humoral immunity.
Dysregulation of TNFRSF13B is linked to immune disorders. Loss-of-function mutations are associated with common variable immunodeficiency (CVID), characterized by impaired antibody production and recurrent infections. Conversely, overactivation of TACI signaling has been implicated in autoimmune diseases, such as systemic lupus erythematosus (SLE), due to excessive B-cell activity.
Recombinant TNFRSF13B protein is engineered by cloning its extracellular domain into expression systems (e.g., mammalian cells, E. coli) to produce soluble, functional forms. This protein retains ligand-binding capacity, enabling research into TACI-ligand interactions, signaling mechanisms, and immune pathway modulation. Therapeutically, recombinant TACI serves as a decoy receptor to neutralize excess BAFF/APRIL, reducing pathogenic B-cell activity in autoimmune conditions. For example, atacicept, a fusion protein combining TACI’s extracellular domain with an immunoglobulin component, has been explored in clinical trials for SLE and rheumatoid arthritis. Additionally, recombinant TNFRSF13B aids in diagnostic assays and drug screening, offering insights into targeted therapies for immune dysregulation. Its production often prioritizes mammalian systems to ensure proper post-translational modifications, enhancing functional reliability.
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