纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | IL22RA1 |
Uniprot No | Q8N6P7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 250-573aa |
氨基酸序列 | SYRYVTKPPAPPNSLNVQRVLTFQPLRFIQEHVLIPVFDLSGPSSLAQPVQYSQIRVSGPREPAGAPQRHSLSEITYLGQPDISILQPSNVPPPQILSPLSYAPNAAPEVGPPSYAPQVTPEAQFPFYAPQAISKVQPSSYAPQATPDSWPPSYGVCMEGSGKDSPTGTLSSPKHLRPKGQLQKEPPAGSCMLGGLSLQEVTSLAMEESQEAKSLHQPLGICTDRTSDPNVLHSGEEGTPQYLKGQLPLLSSVQIEGHPMSLPLQPPSRPCSPSDQGPSPWGLLESLVCPKDEAKSPAPETSDLEQPTELDSLFRGLALTVQWE |
预测分子量 | 50.8 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IL22RA1重组蛋白的参考文献示例(内容基于模拟文献):
1. **"Structural and functional characterization of recombinant IL22RA1 in inflammatory signaling"**
- 作者:Smith A, et al.
- 摘要:研究通过哺乳动物表达系统成功制备重组IL22RA1蛋白,解析其与IL22结合的分子机制,并证实其在体外炎症模型中激活STAT3信号通路的作用。
2. **"IL22RA1 recombinant protein alleviates colitis by modulating epithelial barrier repair"**
- 作者:Chen L, et al.
- 摘要:利用重组IL22RA1蛋白在小鼠结肠炎模型中验证其功能,表明其通过增强肠上皮细胞增殖和黏液分泌,促进黏膜屏障修复。
3. **"Crystal structure of IL22RA1 reveals key residues for cytokine recognition"**
- 作者:Wang Y, et al.
- 摘要:通过X射线晶体学解析重组IL22RA1胞外结构域的三维结构,揭示IL22结合的特异性氨基酸位点,为靶向药物设计提供依据。
4. **"Recombinant IL22RA1-Fc fusion protein inhibits psoriasis-like skin inflammation"**
- 作者:Kim T, et al.
- 摘要:开发IL22RA1-Fc重组融合蛋白,证明其通过竞争性阻断IL22与受体结合,减轻小鼠银屑病模型的皮肤炎症和角质化异常。
(注:以上文献为示例性模拟内容,实际引用时请核实真实文献。)
IL22RA1 (Interleukin-22 Receptor Subunit Alpha 1) is a key component of the interleukin-22 (IL-22) receptor complex, playing a critical role in mediating immune and inflammatory responses. As a type II cytokine receptor, IL22RA1 pairs with IL10RB (Interleukin-10 Receptor Beta) to form a functional heterodimeric receptor capable of binding IL-22. a cytokine produced predominantly by immune cells such as Th17 cells, innate lymphoid cells, and neutrophils. IL-22 signaling is essential for maintaining epithelial barrier integrity, promoting tissue repair, and regulating antimicrobial defense mechanisms, particularly in mucosal surfaces like the gut, skin, and lungs.
The IL22RA1 protein consists of an extracellular domain responsible for ligand binding, a transmembrane domain, and a short intracellular domain lacking intrinsic signaling activity. Instead, downstream signaling—primarily through the JAK-STAT (Janus Kinase-Signal Transducer and Activator of Transcription) pathway—is triggered upon IL-22 binding, leading to STAT3 activation and subsequent transcription of genes involved in cell survival, proliferation, and inflammation. Dysregulation of IL-22/IL22RA1 signaling has been implicated in autoimmune diseases (e.g., psoriasis, inflammatory bowel disease), chronic inflammation, and cancer progression.
Recombinant IL22RA1 proteins are engineered in vitro, often using mammalian expression systems, to retain the native structure and biological activity of the extracellular domain. These proteins serve as research tools to study receptor-ligand interactions, screen therapeutic agents, or modulate IL-22 signaling pathways in experimental models. Additionally, they hold therapeutic potential as decoy receptors to neutralize excessive IL-22 in inflammatory conditions. The development of IL22RA1-targeted biologics highlights its significance as a biomarker and therapeutic target in diseases driven by dysregulated mucosal immunity or tissue damage.
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