| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LILRB3 |
| Uniprot No | O75022 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-443aa |
| 氨基酸序列 | MTPALTALLC LGLSLGPRTR VQAGPFPKPT LWAEPGSVIS WGSPVTIWCQ GSQEAQEYRL HKEGSPEPL DRNNPLEPKN KARFSIPSMT EHHAGRYRCH YYSSAGWSEP SDPLEMVMTG AYSKPTLSA LPSPVVASGG NMTLRCGSQK GYHHFVLMKE GEHQLPRTLD SQQLHSRGFQ ALFPVGPVT PSHRWRFTCY YYYTNTPWVW SHPSDPLEIL PSGVSRKPSL LTLQGPVLAP GQSLTLQCG SDVGYNRFVL YKEGERDFLQ RPGQQPQAGL SQANFTLGPV SPSNGGQYRC YGAHNLSSE WSAPSDPLNI LMAGQIYDTV SLSAQPGPTV ASGENVTLLC QSWWQFDTFL LTKEGAAHP PLRLRSMYGA HKYQAEFPMS PVTSAHAGTY RCYGSYSSNP HLLSHPSEPL ELVVSGHSG GSSLPPTGPP STPGLGRYLE |
| 预测分子量 | 48 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LILRB3重组蛋白的3篇参考文献示例(注：内容为模拟生成，非真实文献)：
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1. **文献名称**：*Structural characterization of recombinant LILRB3 and its interaction with HLA class I molecules*
**作者**：Zhang Y, et al.
**摘要**：本研究通过X射线晶体学解析了重组LILRB3蛋白的胞外结构域，揭示了其与HLA-G的结合界面，为LILRB3在免疫耐受中的调控机制提供结构基础。
2. **文献名称**：*LILRB3 recombinant protein modulates macrophage polarization in tumor microenvironment*
**作者**：Liu X, et al.
**摘要**：实验证明，重组LILRB3蛋白可通过抑制SHP-1/STAT3通路，促进巨噬细胞向M2型极化，从而增强肿瘤免疫逃逸，提示其作为癌症治疗潜在靶点。
3. **文献名称**：*Recombinant LILRB3 inhibits inflammatory response in sepsis models via CD14/TLR4 pathway*
**作者**：Wang H, et al.
**摘要**：在脓毒症小鼠模型中，重组LILRB3蛋白通过阻断CD14与TLR4的相互作用，显著降低促炎因子(如TNF-α、IL-6)水平，缓解全身性炎症反应。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词**"LILRB3 recombinant protein"**，并筛选近五年内发表的实验性研究论文。
**Background of LILRB3 Recombinant Protein**
Leukocyte immunoglobulin-like receptor B3 (LILRB3), also known as ILT5 or CD85a, is a member of the LILR family of immune-regulatory receptors expressed primarily on myeloid cells, such as monocytes, macrophages, and dendritic cells. These receptors play critical roles in modulating immune responses by recognizing major histocompatibility complex (MHC) class I molecules and transmitting inhibitory signals through immunoreceptor tyrosine-based inhibitory motifs (ITIMs) in their cytoplasmic domains. LILRB3. in particular, interacts with HLA-A, HLA-B, and HLA-G antigens, contributing to immune tolerance, suppression of inflammatory reactions, and prevention of autoimmune activation.
Structurally, LILRB3 is a transmembrane glycoprotein composed of extracellular immunoglobulin-like domains, a transmembrane region, and a cytoplasmic tail containing ITIMs. Its recombinant form is typically engineered using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, such as glycosylation, which are essential for ligand binding and functional activity. Recombinant LILRB3 proteins are purified via affinity chromatography, often fused with tags like Fc or His for detection and solubility enhancement.
Research on LILRB3 recombinant protein focuses on its dual role in immunity: dampening excessive immune activation in autoimmune diseases while potentially enabling immune evasion in cancers or chronic infections. Studies explore its therapeutic potential as a checkpoint inhibitor target or a tolerogenic agent in transplantation. Additionally, recombinant LILRB3 serves as a tool to study receptor-ligand interactions, signaling mechanisms, and crosstalk with other immune checkpoints like PD-1/PD-L1. Its applications extend to drug screening, structural biology, and biomarker discovery in diseases such as cancer, rheumatoid arthritis, and sepsis.
In summary, LILRB3 recombinant protein is a pivotal reagent for understanding immune modulation and developing therapies that fine-tune inhibitory pathways in health and disease.
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