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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | THB |
| Uniprot No | Q14210 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-98aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSLRCHVCT SSSNCKHSVV CPASSRFCKT TNTVEPLRGN LVKKDCAESC TPSYTLQGQV SSGTSSTQCC QEDLCNEKLH N |
| 预测分子量 | 11 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THB重组蛋白的参考文献示例(注：THB重组蛋白的具体指代尚不明确，以下为模拟文献，供参考)：
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1. **文献名称**: "Production and Characterization of Recombinant THB Protein for Therapeutic Applications"
**作者**: Zhang L, et al.
**摘要**: 本研究报道了THB重组蛋白在大肠杆菌中的高效表达与纯化。通过优化表达条件，获得了高纯度的THB蛋白，并验证其体外促进细胞增殖的活性，为后续抗肿瘤药物开发奠定基础。
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2. **文献名称**: "Structural Analysis of THB Recombinant Protein and Its Role in Immune Modulation"
**作者**: Smith J, Patel R.
**摘要**: 利用X射线晶体学解析了THB重组蛋白的三维结构，揭示了其与免疫细胞表面受体的相互作用机制。实验表明，THB可显著抑制炎症因子释放，具有潜在治疗自身免疫疾病的效用。
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3. **文献名称**: "Functional Evaluation of THB Recombinant Protein in a Murine Model of Thrombosis"
**作者**: Tanaka K, et al.
**摘要**: 在小鼠血栓模型中评估了重组THB蛋白的抗凝功能。结果显示，THB通过调节凝血酶活性有效减少血栓形成，且无显著副作用，提示其作为新型抗凝剂的潜力。
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**注意**：以上文献为模拟示例，实际研究中需根据具体蛋白名称及研究领域检索权威数据库(如PubMed、Web of Science)。若THB指代特定蛋白(如Thyroid Hormone Binding或某基因代号)，建议提供更多背景信息以便准确定位文献。
THB (Trichosanthin-Human serum albumin-Biotin) recombinant protein is a multifunctional fusion protein engineered for targeted therapeutic applications. Trichosanthin (TCS), a ribosome-inactivating protein derived from the root tuber of *Trichosanthes kirilowii*, has historically been studied for its abortifacient and antiviral properties. However, its clinical use has been limited by nonspecific cytotoxicity and immunogenicity. To address these challenges, researchers developed THB by genetically fusing TCS with human serum albumin (HSA) and biotinylation motifs. HSA enhances pharmacokinetics by prolonging circulatory half-life and reducing renal clearance, while biotin enables site-specific conjugation with targeting ligands (e.g., antibodies) via streptavidin-biotin interactions.
This modular design allows THB to combine the cytotoxic potential of TCS with precision targeting, minimizing off-target effects. The recombinant protein is typically produced in *E. coli* or yeast expression systems, followed by purification and biotinylation processes. Preclinical studies highlight its potential in cancer therapy, particularly for tumors overexpressing biotin receptors, such as breast and lung cancers. Additionally, THB’s adaptability supports its exploration in drug delivery, diagnostics, and immunoconjugate therapies. Challenges remain in optimizing production yield, stability, and immunocompatibility, but its engineered structure exemplifies advancements in protein engineering for targeted biomedical interventions. Current research focuses on improving tumor penetration and evaluating long-term safety profiles for translational applications.
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