| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IREM1 |
| Uniprot No | Q8TDQ1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-156aa |
| 氨基酸序列 | TQITGPTTVNGLERGSLTVQCVYRSGWETYLKWWCRGAIWRDCKILVKTSGSEQEVKRDRVSIKDNQKNRTFTVTMEDLMKTDADTYWCGIEKTGNDLGVTVQVTIDPAPVTQEETSSSPTLTGHHLDNRHKLLKLS |
| 预测分子量 | 17.5 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IREM1重组蛋白的3篇示例参考文献(内容为示例性概括，非真实文献)：
1. **《IREM1重组蛋白的分子特性及免疫调节功能研究》**
- 作者：Smith A, et al.
- 摘要：本研究通过大肠杆菌表达系统成功制备了重组IREM1蛋白，并验证其与TREM家族受体的相互作用。实验表明，IREM1通过抑制NF-κB通路调控巨噬细胞的炎症反应，提示其在自身免疫疾病中的潜在治疗价值。
2. **《重组IREM1蛋白的结构解析及其配体结合机制》**
- 作者：Zhang L, et al.
- 摘要：通过X射线晶体学解析了重组IREM1胞外结构域的3D结构，发现其免疫球蛋白样结构域包含关键配体结合位点。进一步功能实验证实，重组IREM1可特异性结合病原体相关分子模式(PAMPs)，增强吞噬细胞清除病原体的能力。
3. **《IREM1重组蛋白在脓毒症模型中的保护作用》**
- 作者：Wang Y, et al.
- 摘要：在脓毒症小鼠模型中，外源性重组IREM1蛋白显著降低了血清炎症因子(如TNF-α、IL-6)水平，并改善器官损伤。研究揭示了IREM1通过调控TLR4信号通路抑制过度炎症反应的分子机制。
4. **《高效表达及纯化哺乳动物细胞源的IREM1重组蛋白》**
- 作者：Chen R, et al.
- 摘要：开发了一种基于HEK293细胞的重组IREM1蛋白表达体系，通过亲和层析和尺寸排阻色谱获得高纯度蛋白。功能实验显示，哺乳动物源IREM1较原核表达产物具有更优的糖基化修饰及生物活性。
(注：以上为模拟文献，实际研究需通过PubMed、Google Scholar等平台检索具体论文。)
**Background of Recombinant IREM1 Protein**
IREM1 (Immune Receptor Expressed on Myeloid cells 1), also known as CD300LF, is a cell surface glycoprotein belonging to the CD300 family of immunoregulatory receptors. It is primarily expressed on myeloid cells, including macrophages, dendritic cells, and neutrophils, where it modulates immune responses through interactions with lipid ligands or pathogen-associated molecules. IREM1 contains immunoreceptor tyrosine-based inhibitory motifs (ITIMs) in its cytoplasmic domain, enabling it to transduce inhibitory signals that regulate cellular activation, cytokine production, and phagocytosis.
Recombinant IREM1 protein is engineered to study its structural and functional properties in vitro or in vivo. It is typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation, which is critical for ligand binding and receptor stability. The purified protein often includes extracellular domains to facilitate ligand interaction studies, receptor dimerization analysis, or antibody development.
Research on recombinant IREM1 has highlighted its role in balancing immune activation and tolerance. For instance, it inhibits excessive inflammation by suppressing TLR (Toll-like receptor) signaling in sepsis models and modulates antitumor immunity by interacting with phosphatidylserine on apoptotic cells. Dysregulation of IREM1 is linked to autoimmune diseases, chronic infections, and cancer progression, making it a potential therapeutic target. Current applications include screening for small-molecule inhibitors, designing fusion proteins for immune modulation, and exploring its diagnostic value in inflammatory disorders.
Overall, recombinant IREM1 serves as a vital tool for dissecting immune checkpoint mechanisms and developing targeted therapies in immunology and oncology.
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