| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GAL3 |
| Uniprot No | P17931 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-250aa |
| 氨基酸序列 | ADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI |
| 预测分子量 | 26.0 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GAL3(半乳糖凝集素-3)重组蛋白的模拟参考文献示例，供参考：
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1. **标题**：*Expression and purification of recombinant human galectin-3 for structural studies*
**作者**：Smith A, et al.
**摘要**：研究报道了通过大肠杆菌系统高效表达可溶性重组人GAL3蛋白的方法，并利用亲和层析技术纯化，获得高纯度蛋白用于X射线晶体学分析，揭示了其CRD结构域的关键结合位点。
2. **标题**：*Functional characterization of recombinant galectin-3 in cancer cell adhesion*
**作者**：Chen L, et al.
**摘要**：通过哺乳动物细胞表达系统制备重组GAL3.证明其通过调节β-catenin信号通路增强肿瘤细胞黏附能力，为GAL3在肿瘤转移中的作用提供机制依据。
3. **标题**：*Role of recombinant galectin-3 in modulating macrophage polarization*
**作者**：Kim J, et al.
**摘要**：利用昆虫细胞表达的重组GAL3蛋白，发现其通过TLR4/NF-κB通路促进巨噬细胞向M2型极化，提示其在炎症性疾病中的潜在治疗靶点。
4. **标题**：*Development of a galectin-3 inhibitor screening assay using recombinant protein*
**作者**：Wang Y, et al.
**摘要**：基于重组GAL3蛋白建立高通量抑制剂筛选平台，筛选出小分子化合物MB-10可特异性阻断GAL3与配体结合，为纤维化疾病药物开发提供工具。
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注：以上文献为模拟示例，实际引用需以真实出版物为准。建议通过PubMed或Web of Science以“recombinant galectin-3”为关键词检索最新研究。
Galectin-3 (GAL3), a member of the lectin family, is a multifunctional β-galactoside-binding protein implicated in diverse cellular processes, including cell adhesion, apoptosis, immune regulation, and intracellular signaling. Structurally, it consists of an N-terminal proline-rich domain that enables oligomerization and a C-terminal carbohydrate recognition domain (CRD) responsible for ligand binding. Unlike other galectins, GAL3 exists in both soluble and membrane-associated forms, allowing it to interact with extracellular glycoproteins, cell surface receptors, and intracellular targets. Its expression is upregulated in various pathological conditions, such as cancer metastasis, fibrosis, chronic inflammation, and cardiovascular diseases, making it a biomarker and therapeutic target of interest.
Recombinant GAL3 protein is typically produced using expression systems like *E. coli* or mammalian cell lines to ensure proper folding and post-translational modifications. Purification often involves affinity chromatography leveraging its lactose-binding properties. In research, recombinant GAL3 is utilized to study its role in mediating cell-cell interactions, modulating immune responses, and promoting tumor progression through mechanisms like angiogenesis and evasion of apoptosis. For instance, it binds to ligands such as laminin, integrins, and MUC1 to facilitate cancer cell adhesion and metastasis. In fibrosis, GAL3 drives fibroblast activation and collagen deposition, while in inflammation, it regulates neutrophil recruitment and cytokine production.
Therapeutic strategies targeting GAL3 include small-molecule inhibitors, monoclonal antibodies, and carbohydrate-based antagonists. These aim to disrupt its pathological interactions in diseases like diabetic nephropathy, hepatic fibrosis, and certain cancers. Additionally, recombinant GAL3 serves as a tool for diagnostic assays, vaccine development, and elucidating structure-function relationships. Despite its pleiotropic roles, challenges remain in understanding context-dependent mechanisms and minimizing off-target effects in therapies. Ongoing research continues to unravel its dual roles as a damage-associated molecular pattern (DAMP) and a regulator of tissue homeostasis.
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