| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SIRPb1 |
| Uniprot No | O00241 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-181aa |
| 氨基酸序列 | MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESA TLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNN LDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVREPALAP TAPLLVALLLGPKLLLVVGVSAIYICWKQKA |
| 预测分子量 | 43,2 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SIRPβ1重组蛋白的3篇参考文献及其摘要内容概括：
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1. **文献名称**: *"Recombinant SIRPβ1 protein blocks CD47 signaling to enhance macrophage phagocytosis in cancer immunotherapy"*
**作者**: Zhang Y, et al.
**摘要**: 研究团队通过表达纯化重组SIRPβ1胞外段蛋白，验证其与CD47的结合能力，并证明该蛋白可阻断肿瘤细胞表面CD47的“别吃我”信号，显著增强巨噬细胞对肿瘤细胞的吞噬作用，为癌症免疫治疗提供新策略。
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2. **文献名称**: *"Structural and functional characterization of recombinant human SIRPβ1 for immune checkpoint modulation"*
**作者**: Liu X, et al.
**摘要**: 解析了重组人源SIRPβ1蛋白的晶体结构，揭示其与CD47相互作用的关键表位;体外实验表明，重组SIRPβ1通过激活DAP12通路增强NK细胞的抗肿瘤活性，提示其作为免疫检查点调节剂的潜力。
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3. **文献名称**: *"Engineering a high-affinity SIRPβ1 recombinant protein to enhance antitumor immunity"*
**作者**: Wang H, et al.
**摘要**: 通过定向进化技术优化重组SIRPβ1的亲和力，获得突变体SIRPβ1-Fc。该蛋白在小鼠模型中显著抑制肿瘤生长，并促进T细胞浸润，表明其通过双重调节先天性和适应性免疫发挥抗肿瘤作用。
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(注：以上文献为示例性概括，实际文献需通过PubMed/Google Scholar检索确认。)
The signal regulatory protein beta 1 (SIRPβ1), also known as SIRPβ or CD172b, is a member of the SIRP family of transmembrane glycoproteins involved in immune regulation. Structurally, SIRPβ1 belongs to the immunoglobulin (Ig) superfamily, featuring extracellular Ig-like domains that mediate ligand interactions. Unlike its well-studied homolog SIRPα (CD172a), which contains immunoreceptor tyrosine-based inhibitory motifs (ITIMs) for downstream signaling, SIRPβ1 lacks intracellular signaling domains but associates with adaptor proteins like DAP12 to activate immune cells.
SIRPβ1 is predominantly expressed on myeloid cells, such as dendritic cells and macrophages, and interacts with CD47. a widely distributed "don’t eat me" signal ligand. This interaction modulates phagocytosis, inflammation, and T-cell activation, positioning SIRPβ1 as a critical checkpoint in innate and adaptive immunity. Recent studies highlight its role in cancer immune evasion, where CD47-SIRPβ1 signaling inhibits macrophage-mediated tumor cell clearance.
Recombinant SIRPβ1 proteins are engineered *in vitro* using expression systems (e.g., mammalian or insect cells) to preserve post-translational modifications and ligand-binding capacity. These proteins serve as tools to study CD47-SIRP pathway dynamics, screen therapeutic antibodies, or develop decoy receptors to block immunosuppressive signals. In cancer immunotherapy, targeting SIRPβ1-CD47 axis has emerged as a strategy to enhance phagocytosis of malignant cells, with recombinant variants aiding in structure-function analyses and preclinical validation. Further research explores its involvement in inflammatory diseases, underscoring its dual role as a regulator of immune tolerance and activation.
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