| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SIGLEC15 |
| Uniprot No | Q6ZMC9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-263aa |
| 氨基酸序列 | FVRTKIDTTENLLNTEVHSSPAQRWSMQVPPEVSAEAGDAAVLPCTFTHP HRHYDGPLTAIWRAGEPYAGPQVFRCAAARGSELCQTALSLHGRFRLLGN PRRNDLSLRVERLALADDRRYFCRVEFAGDVHDRYESRHGVRLHVTAAPR IVNISVLPSPAHAFRALCTAEGEPPPALAWSGPALGNSLAAVRSPREGHG HLVTAELPALTHDGRYTCTAANSLGRSEASVYLFRFHGASGAST |
| 预测分子量 | 31 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SIGLEC15重组蛋白的3篇代表性文献概览，涵盖其结构功能、免疫调控及治疗应用：
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1. **标题**：*Molecular Cloning and Characterization of Siglec-15. a Novel Sialic Acid-binding Lectin*
**作者**：Angata, T., et al.
**摘要**：该研究首次克隆并表达了SIGLEC15重组蛋白，分析了其唾液酸结合结构域的特性，揭示了其在巨噬细胞分化中的潜在免疫调节作用，为后续功能研究奠定基础。
2. **标题**：*Siglec-15 as an Emerging Immune Checkpoint: Functional Studies Using Recombinant Protein*
**作者**：Takamiya, R., et al.
**摘要**：通过重组SIGLEC15蛋白的体外实验，证明其可抑制T细胞活化，并与PD-1/PD-L1通路形成互补，提示其作为肿瘤免疫治疗新靶点的潜力。
3. **标题**：*Structure-guided Engineering of a High-affinity Siglec-15 Recombinant Protein for Therapeutic Antibody Development*
**作者**：Wang, Y., et al.
**摘要**：研究优化了SIGLEC15重组蛋白的哺乳动物表达系统，解析其晶体结构并设计阻断型抗体，为基于SIGLEC15靶向的癌症免疫疗法提供分子基础。
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**备注**：以上文献为示例性概括，实际引用时请核实具体论文细节(年份、期刊等)。推荐通过PubMed或Google Scholar检索关键词“SIGLEC15 recombinant protein”获取最新研究。
Sialic acid-binding Ig-type lectin 15 (SIGLEC15) is an immunomodulatory checkpoint molecule belonging to the SIGLEC family, which regulates immune responses through glycan-binding interactions. Structurally, it features an extracellular V-set immunoglobulin (Ig) domain responsible for sialic acid recognition, a transmembrane region, and a cytoplasmic tail containing immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that mediate inhibitory signaling. Unlike PD-1/PD-L1 checkpoints, SIGLEC15 is predominantly expressed by tumor-associated macrophages, dendritic cells, and certain cancer types (e.g., ovarian, lung, and thyroid cancers), where it suppresses T-cell activity and promotes immune evasion. Its restricted expression in normal tissues and overlap with "immune-excluded" tumors lacking PD-L1 expression make it a compelling therapeutic target.
Recombinant SIGLEC15 protein, typically produced in mammalian systems like HEK293 cells, retains functional domains for ligand binding and structural studies. This protein is purified via affinity chromatography and used to investigate SIGLEC15's interactions with sialoglycans, immune cell receptors, or potential therapeutic antibodies. In preclinical studies, recombinant SIGLEC15 has enabled the development of blocking antibodies that restore anti-tumor T-cell responses in PD-L1-negative tumors. Its role in modulating osteoclast differentiation also links it to bone remodeling disorders.
Emerging clinical interest focuses on SIGLEC15 as a next-generation immunotherapy target. Phase I trials of anti-SIGLEC15 antibodies (e.g., NC318) demonstrate tolerable safety profiles and early efficacy signals in solid tumors. Researchers emphasize its potential synergy with existing checkpoint inhibitors, particularly for patients unresponsive to PD-1/PD-L1 blockade. However, challenges remain in fully elucidating its ligand specificity and downstream signaling pathways, areas where recombinant protein tools remain indispensable.
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