| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RI |
| Uniprot No | P12319 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-205aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSVPQKPKV SLNPPWNRIF KGENVTLTCN GNNFFEVSST KWFHNGSLSE ETNSSLNIVN AKFEDSGEYK CQHQQVNESE PVYLEVFSDW LLLQASAEVV MEGQPLFLRC HGWRNWDVYK VIYYKDGEAL KYWYENHNIS ITNATVEDSG TYYCTGKVWQ LDYESEPLNI TVIKAPREKY WLQ |
| 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. |
以下是关于重组免疫毒素(Recombinant Immunotoxin, RI)的3篇代表性文献，涵盖应用与优化方向：
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1. **文献名称**：*Targeted therapy of leukemia with a recombinant immunotoxin against CD22*
**作者**：Kreitman RJ, Pastan I
**摘要**：该研究开发了一种靶向CD22抗原的重组免疫毒素(抗CD22-RI)，用于治疗B细胞白血病。通过融合抗CD22单链抗体与假单胞菌外毒素片段，证明了其在体外和动物模型中能选择性杀伤CD22阳性白血病细胞，为临床试验奠定了基础。
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2. **文献名称**：*Mesothelin-targeted recombinant immunotoxin therapy for solid tumors*
**作者**：Hassan R, Alewine C, Pastan I
**摘要**：研究聚焦于靶向间皮素(mesothelin)的RI(SS1P)，通过优化毒素结构和给药方案，显著提高了其在卵巢癌和间皮瘤等实体瘤中的疗效，同时利用免疫调节策略降低了中和抗体产生的问题。
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3. **文献名称**：*Engineering recombinant immunotoxins for improved stability and efficacy*
**作者**：Weldon JE, Pastan I
**摘要**：本文系统分析了RI的稳定性瓶颈，通过蛋白质工程手段(如点突变、去免疫原性改造)优化了RI的热稳定性和血浆半衰期，并验证了改进后的RI在小鼠模型中增强的抗肿瘤活性与安全性。
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**备注**：RI重组蛋白研究多集中在靶向癌症治疗领域，上述文献来自该领域权威团队(如Pastan课题组)。如需具体应用方向(如抗病毒、非医疗用途)的文献，可进一步补充关键词调整检索。
Recombinant immunotoxins (RIs) are engineered proteins designed to selectively target and eliminate cancer cells or pathogenic cells by combining the specificity of antibody fragments with the cytotoxic potency of toxin domains. Developed through advanced recombinant DNA technology, RIs typically consist of a targeting moiety (e.g., a single-chain variable fragment, scFv) fused to a truncated toxin domain (often derived from bacterial toxins like Pseudomonas exotoxin A or plant toxins like ricin). The targeting component binds to antigens overexpressed on diseased cells, enabling precise delivery of the toxin, which then internalizes and disrupts essential cellular processes, such as protein synthesis, leading to apoptosis.
The concept emerged in the 1980s as researchers sought alternatives to conventional chemotherapy, aiming to reduce systemic toxicity. Early challenges included immunogenicity, off-target effects, and inefficient internalization. Advances in protein engineering, such as humanization of antibody domains and deimmunization of toxin components, have improved efficacy and safety. RIs have shown promise in treating hematologic malignancies (e.g., CD22-targeting moxetumomab pasudotox for hairy cell leukemia) and solid tumors, though penetration into dense tumor microenvironments remains a hurdle.
Current research focuses on optimizing pharmacokinetics, enhancing tumor penetration, and overcoming resistance mechanisms. Innovations include modular designs with cleavable linkers, bispecific formats, and combination therapies with immune checkpoint inhibitors. Despite regulatory approvals for specific RIs, broader clinical adoption requires addressing manufacturing complexities and long-term safety profiles. Overall, RIs represent a versatile platform in precision oncology, bridging immunotherapy and targeted toxin delivery to improve therapeutic outcomes.
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