纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CD59A |
Uniprot No | P13987 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-102aa |
氨基酸序列 | MASMTGGQQMGRGHHHHHHGNLYFQGGEFALVQCYNCPNPTADCKTAVNC SSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLC NFNEQLEN |
预测分子量 | 12 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CD59A重组蛋白的模拟参考文献(内容基于常见研究方向整合,非真实文献):
1. **"Expression and Functional Characterization of Recombinant Human CD59 in HEK293 Cells"**
- 作者:Smith J, et al.
- 摘要:研究通过哺乳动物表达系统(HEK293)重组表达人CD59蛋白,分析其糖基化修饰对补体抑制活性的影响,证实糖基化对蛋白稳定性及功能的关键作用。
2. **"Bacterial Expression and Purification of Mouse CD59A for Structural Studies"**
- 作者:Li X, et al.
- 摘要:利用大肠杆菌系统表达小鼠CD59A重组蛋白,通过优化纯化工艺获得高纯度蛋白,并解析其晶体结构,揭示其与补体C8/C9结合的分子机制。
3. **"Recombinant CD59A Protects Neuronal Cells from Complement-Mediated Lysis in Neuroinflammatory Models"**
- 作者:Wang Y, et al.
- 摘要:评估重组CD59A在神经炎症疾病模型中的保护作用,证明其通过抑制补体膜攻击复合物形成,减少神经元损伤,提示其治疗潜力。
4. **"Engineering a Soluble Form of CD59A for Therapeutic Applications in Autoimmune Disorders"**
- 作者:Brown K, et al.
- 摘要:通过基因工程技术改造小鼠CD59A,开发可溶性重组蛋白变体,并在体外和动物模型中验证其抑制补体过度激活的能力,为自身免疫病治疗提供新策略。
(注:以上文献为示例性内容,实际研究需参考真实数据库如PubMed、Web of Science。)
CD59A, also known as CD59 glycoprotein or protectin, is a membrane-anchored regulatory protein that plays a critical role in inhibiting the complement system's terminal pathway. As a key complement defense protein, it prevents the formation of the membrane attack complex (MAC) by binding to C8 and C9 components during MAC assembly on host cell surfaces. This activity protects human cells from unintended complement-mediated lysis, making CD59A essential for maintaining cellular integrity in physiological conditions.
The recombinant CD59A protein is produced through genetic engineering techniques, typically expressed in mammalian cell systems (e.g., CHO cells) or bacterial systems using E. coli. The recombinant form retains the functional domain of native CD59 (60-77 amino acid residues in the mature protein) while often being engineered without the glycosylphosphatidylinositol (GPI) anchor for improved solubility and purification. This modification allows researchers to study its inhibitory mechanism and therapeutic potential more effectively.
In research applications, recombinant CD59A serves as a valuable tool for investigating complement-related disorders such as paroxysmal nocturnal hemoglobinuria (PNH), age-related macular degeneration, and ischemia-reperfusion injuries. Therapeutic development focuses on its potential for treating complement-mediated diseases, either through direct administration or as a fusion protein construct. Recent studies also explore its role in immune modulation beyond complement regulation, including possible interactions with T-cell receptors and signaling pathways in inflammatory conditions.
The production of recombinant CD59A has enabled structural studies using X-ray crystallography and NMR, revealing its characteristic disc-shaped β-sandwich fold stabilized by disulfide bonds. These structural insights guide the design of modified variants with enhanced stability or targeted specificity. Current challenges in therapeutic applications include optimizing its pharmacokinetic profile and overcoming potential immunogenicity, while diagnostic applications leverage recombinant CD59A as a standard in flow cytometry for PNH testing.
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