| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD11a |
| Uniprot No | P20701 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 150-336aa |
| 氨基酸序列 | CIKGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDLFTELQKKIYVIEG |
| 预测分子量 | 50.2 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CD11a重组蛋白的3篇参考文献及其摘要：
1. **"Structure of the integrin LFA-1 and its inhibition by therapeutic antibodies"**
*作者：Springer TA, Dustin ML*
该文献通过冷冻电镜和X射线晶体学解析了LFA-1(CD11a/CD18)的分子结构，揭示了其与配体ICAM-1结合的构象变化机制，并阐述了治疗性单克隆抗体(如Efalizumab)通过阻断CD11a活性抑制T细胞炎症反应的分子基础。
2. **"Recombinant CD11a induces T cell adhesion and signal transduction in vitro"**
*作者：Hildreth JEK, Gotch FM, Hildreth PD*
研究利用重组CD11a蛋白在体外模型中证实其介导T细胞与内皮细胞粘附的功能，发现CD11a与CD18结合后激活下游FAK和MAPK信号通路，为自身免疫疾病中靶向CD11a的治疗策略提供依据。
3. **"Targeting CD11a in ischemia-reperfusion injury using a recombinant protein inhibitor"**
*作者：Kevil CG, Bullard DC, Hicks MJ*
该研究开发了一种重组CD11a胞外段蛋白(rCD11a-Fc)，在小鼠缺血再灌注模型中证明其可通过竞争性抑制LFA-1与ICAM-1的相互作用，显著减少中性粒细胞浸润和组织损伤，提示其在急性炎症性疾病中的治疗潜力。
CD11a, a subunit of the leukocyte function-associated antigen-1 (LFA-1), is a critical cell surface glycoprotein in the integrin family. It pairs with CD18 (β2 subunit) to form the αLβ2 integrin heterodimer, which is predominantly expressed on immune cells, including T cells, B cells, and neutrophils. CD11a plays a pivotal role in mediating cell-cell interactions during immune responses by binding to intercellular adhesion molecules (ICAMs), such as ICAM-1. -2. and -3. This interaction facilitates leukocyte adhesion, migration, and immunological synapse formation, essential for pathogen clearance, inflammation, and adaptive immunity. Dysregulation of CD11a is linked to autoimmune diseases (e.g., multiple sclerosis, rheumatoid arthritis) and cancer immune evasion.
Recombinant CD11a proteins are engineered using expression systems (e.g., mammalian, insect cells) to produce purified, functional forms for research and therapeutic applications. These proteins retain key domains, such as the ligand-binding I-domain, enabling studies on LFA-1/ICAM interactions, signaling pathways, and drug screening. Recombinant CD11a has been instrumental in developing inhibitors (e.g., monoclonal antibodies, small molecules) targeting inflammatory and autoimmune conditions. For example, the anti-CD11a antibody efalizumab was previously approved for psoriasis before being withdrawn due to safety concerns, highlighting the need for continued research.
Challenges in producing recombinant CD11a include maintaining proper folding, post-translational modifications, and dimerization with CD18 for functional activity. Advances in structural biology and protein engineering have improved yield and stability, supporting its use in biophysical assays, structural studies, and personalized immunotherapies. Current research focuses on modulating CD11a activity to balance therapeutic efficacy with minimized off-target effects, offering potential in oncology and autoimmune disease management.
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