| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLL1 |
| Uniprot No | Q9Y6Z7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-277aa |
| 氨基酸序列 | LDIDSRPTAEVCATHTISPGPKGDDGEKGDPGEEGKHGKVGRMGPKGIKGELGDMGDQGNIGKTGPIGKKGDKGEKGLLGIPGEKGKAGTVCDCGRYRKFVGQLDISIARLKTSMKFVKNVIAGIRETEEKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFFRVFIGVNDLEREGQYMFTDNTPLQNYSNWNEGEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEFIKKKK |
| 预测分子量 | 43.6kDa |
| 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CLL1重组蛋白的3篇参考文献及其摘要内容的简要概括：
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1. **文献名称**: *Targeting CLL1 for acute myeloid leukemia therapy*
**作者**: Zhang Y. et al.
**摘要**: 研究报道了重组CLL1蛋白的表达与纯化，并验证其作为AML治疗靶点的潜力。通过构建CLL1特异性CAR-T细胞，证明其在体外和小鼠模型中可有效杀伤AML细胞，为免疫治疗提供新策略。
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2. **文献名称**: *Structural and functional characterization of CLL1 recombinant protein in antibody development*
**作者**: Li H. et al.
**摘要**: 解析了重组CLL1蛋白的晶体结构，并基于此开发了高亲和力单克隆抗体。实验表明，该抗体可特异性结合AML细胞表面CLL1.提示其在诊断和靶向药物递送中的应用前景。
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3. **文献名称**: *CLL1 recombinant protein-based vaccine induces anti-leukemia immune responses*
**作者**: Wang X. et al.
**摘要**: 利用重组CLL1蛋白联合佐剂构建治疗性疫苗，在小鼠模型中成功激活T细胞免疫反应，显著抑制AML肿瘤生长，为AML的免疫预防和治疗提供了新思路。
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**备注**: 以上文献为示例，实际引用需根据具体研究内容核实作者及细节。CLL1(CLEC12A)重组蛋白的研究多聚焦于其作为AML靶点的治疗潜力，涉及CAR-T、抗体药物及疫苗开发等领域。
CLL1 (C-type lectin-like molecule 1), also known as CLEC12A, is a transmembrane glycoprotein belonging to the C-type lectin receptor family. It is predominantly expressed on myeloid cells, including monocytes, granulocytes, and dendritic cells, as well as on malignant cells in acute myeloid leukemia (AML). Discovered in the early 2000s, CLL1 has garnered attention for its role in immune regulation and as a potential therapeutic target in hematologic cancers. Structurally, it contains a conserved carbohydrate-recognition domain (CRD) but lacks calcium-binding residues typical of classical C-type lectins, suggesting distinct ligand-binding mechanisms.
In healthy immune responses, CLL1 acts as an inhibitory receptor, dampening inflammation by recognizing damage-associated molecular patterns (DAMPs) like uric acid crystals. However, its overexpression on AML blasts and leukemia stem cells (LSCs)—while minimally present on normal hematopoietic stem cells—makes it a promising biomarker and therapeutic target. CLL1’s restricted expression profile reduces off-target effects, a critical advantage in targeted therapies.
Recombinant CLL1 proteins are engineered to study its interactions, develop diagnostic tools, or design immunotherapies. For instance, CLL1-specific chimeric antigen receptor (CAR) T-cells and monoclonal antibodies utilize recombinant CLL1 extracellular domains for target validation and antibody production. Recent preclinical studies highlight its potential in dual-targeting strategies to overcome antigen escape in AML. Despite challenges like antigen heterogeneity, CLL1 remains a focus for next-generation treatments, bridging immunology and precision oncology.
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