| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC12A |
| Uniprot No | Q5QGZ9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-265aa |
| 氨基酸序列 | MSEEVTYADLQFQNSSEMEKIPEIGKFGEKAPPAPSHVWRPAALFLTLLCLLLLIGLGVLASMFHVTLKIEMKKMNKLQNISEELQRNISLQLMSNMNISNKIRNLSTTLQTIATKLCRELYSKEQEHKCKPCPRRWIWHKDSCYFLSDDVQTWQESKMACAAQNASLLKINNKNALEFIKSQSRSYDYWLGLSPEEDSTRGMRVDNIINSSAWVIRNAPDLNNMYCGYINRLYVQYYHCTYKKRMICEKMANPVQLGSTYFREA |
| 预测分子量 | 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CLEC12A重组蛋白的3篇模拟参考文献示例(基于学术知识框架，非真实文献)：
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1. **标题**：Structural characterization of the human CLEC12A extracellular domain reveals a conserved C-type lectin fold
**作者**：Van der Meer, J.W. et al.
**摘要**：本研究通过X射线晶体学解析了人源CLEC12A重组蛋白胞外结构域的三维结构，揭示了其典型的C型凝集素折叠模式，并鉴定出潜在的配体结合位点，为理解其免疫调控机制提供了结构基础。
2. **标题**：CLEC12A recognizes endogenous danger signals and suppresses neutrophil activation
**作者**：Neumann, K. et al.
**摘要**：研究证明CLEC12A重组蛋白可特异性结合细胞损伤释放的尿酸结晶等内源性危险分子，通过抑制中性粒细胞过度活化负向调节炎症反应，提示其在自身免疫疾病中的潜在治疗价值。
3. **标题**：Targeting CLEC12A with recombinant antibodies enhances anti-leukemia immune responses
**作者**：Bakker, A.B.H. et al.
**摘要**：开发了靶向CLEC12A的重组单克隆抗体，体外实验证实其可特异性结合急性髓系白血病细胞表面CLEC12A，并促进巨噬细胞吞噬作用，为基于CLEC12A的肿瘤免疫治疗提供了新策略。
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**说明**：以上文献为示例性内容，实际引用时建议通过PubMed或Web of Science以"CLEC12A recombinant protein"、"CLEC12A structure/function"等关键词检索近年高被引论文。真实研究多聚焦于其作为免疫检查点的调控机制及肿瘤靶向治疗应用。
CLEC12A (C-type lectin domain family 12 member A), also known as MICL (myeloid inhibitory C-type lectin-like receptor) or CLLEC12A, is a transmembrane protein belonging to the C-type lectin receptor (CLR) family. It is primarily expressed on myeloid cells, including monocytes, macrophages, dendritic cells, and neutrophils, and plays a regulatory role in immune responses. Structurally, CLEC12A features an extracellular C-type lectin-like domain responsible for ligand recognition, a transmembrane domain, and a cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM) that mediates inhibitory signaling.
Functionally, CLEC12A acts as a pattern recognition receptor (PRR) that detects damage-associated molecular patterns (DAMPs), particularly uric acid crystals and other necrotic cell-derived signals. Upon ligand binding, its ITIM domain recruits phosphatases (e.g., SHP-1/SHP-2) to dampen activating signals from other immune receptors, thereby preventing excessive inflammation and maintaining immune homeostasis. This inhibitory mechanism helps balance immune activation and tolerance, making CLEC12A a critical checkpoint in myeloid cell regulation.
CLEC12A has garnered attention in disease research, particularly in oncology and hematology. It is overexpressed in certain leukemias, including acute myeloid leukemia (AML), where it serves as a potential therapeutic target. Antibody-drug conjugates (ADCs) and CAR-T cell therapies targeting CLEC12A are under investigation for leukemia treatment. Additionally, its role in modulating inflammatory responses links it to autoimmune disorders and chronic inflammatory conditions.
Recombinant CLEC12A proteins, typically produced in mammalian expression systems to ensure proper glycosylation and folding, are widely used in vitro to study ligand-receptor interactions, immune signaling pathways, and drug screening. These tools have advanced the development of diagnostic antibodies and therapeutic agents aimed at manipulating CLEC12A activity in pathological contexts. Ongoing research continues to explore its dual role as both a sensor of cellular stress and a regulator of immune activation.
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