| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC3A |
| Uniprot No | O75596 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-197aa |
| 氨基酸序列 | MAKNGLVICILVITLLLDQTTSHTSRLKARKHSKRRVRDKDGDLKTQIEKLWTEVNALKEIQALQTVCLRGTKVHKKCYLASEGLKHFHEANEDCISKGGILVIPRNSDEINALQDYGKRSLPGVNDFWLGINDMVTEGKFVDVNGIAISFLNWDRAQPNGGKRENCVLFSQSAQGKWSDEACRSSKRYICEFTIPK |
| 分子量 | 48.6 KDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是基于文献知识模拟生成的关于重组人CLEC3A蛋白的参考文献示例(非真实存在，仅供参考)：
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1. **Title**: Recombinant human CLEC3A protein inhibits tumor angiogenesis through integrin interaction
**Authors**: Zhang L, et al.
**Summary**: 本研究利用哺乳动物系统表达重组人CLEC3A蛋白，发现其通过结合内皮细胞表面整合素αvβ3抑制VEGF信号通路，显著降低体外血管生成能力，提示其在抗肿瘤治疗中的潜在应用。
2. **Title**: Structural characterization of CLEC3A and its carbohydrate-binding specificity
**Authors**: Tanaka K, et al.
**Summary**: 通过X射线晶体学解析重组CLEC3A蛋白的C型凝集素结构域，揭示其对半乳糖修饰糖链的特异性结合模式，为研究其免疫调节功能提供结构基础。
3. **Title**: CLEC3A as a novel biomarker in hepatocellular carcinoma: Expression and functional analysis
**Authors**: Wang Y, et al.
**Summary**: 利用重组CLEC3A蛋白验证其在肝癌细胞中的表达下调现象，并通过体外实验证明其过表达可抑制肝癌细胞迁移和侵袭，机制可能与Wnt/β-catenin通路相关。
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**建议**：
- 实际文献需通过PubMed (https://pubmed.ncbi.nlm.nih.gov) 或Google Scholar检索关键词(如 "recombinant CLEC3A"、"CLEC3A function")。
- 关注近年发表的文献(如2020年后)，以获取领域最新进展。
- 可结合CLEC3A相关研究领域(如癌症、骨代谢、先天免疫)细化检索方向。
Recombinant human CLEC3A (C-type lectin domain family 3 member A) is a protein derived from the CLEC3A gene, part of the C-type lectin superfamily known for carbohydrate-binding capabilities. CLEC3A, also termed tetranectin, is a secreted glycoprotein implicated in diverse physiological processes, including tissue remodeling, cell adhesion, and modulation of extracellular matrix (ECM) interactions. Structurally, it contains a C-terminal carbohydrate recognition domain (CRD) that facilitates binding to plasminogen and sulfated polysaccharides, influencing proteolytic pathways and ECM organization.
Recombinant CLEC3A is typically produced using expression systems like mammalian cells or bacteria, enabling controlled studies of its biological roles. Research highlights its involvement in cancer progression, osteogenesis, and neurological disorders, as it regulates matrix metalloproteinases (MMPs) and interacts with growth factors like TGF-β. CLEC3A’s dysregulation has been linked to tumor metastasis, bone density alterations, and neurodegenerative conditions, underscoring its therapeutic potential. Its recombinant form is instrumental in elucidating mechanisms of ECM dynamics, developing diagnostic biomarkers, and exploring targeted therapies. Despite progress, its precise signaling pathways and tissue-specific functions remain under investigation, necessitating further studies to unlock its full clinical relevance.
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