| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Lgals3 |
| 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3篇关于LGALS3(Galectin-3)重组蛋白的经典研究文献及其摘要概括：
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1. **文献名称**: *Galectin-3: A Novel Antiapoptotic Molecule with a Functional BH1 Domain*
**作者**: Yu F, et al.
**摘要**: 研究证明重组Galectin-3蛋白通过其BH1结构域抑制细胞凋亡，在肿瘤细胞中通过调控线粒体途径增强生存能力，为癌症治疗的靶点提供了新依据。
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2. **文献名称**: *Role of Galectin-3 in Hepatic Fibrosis*
**作者**: Henderson NC, et al.
**摘要**: 利用重组Galectin-3蛋白实验，揭示了其在肝纤维化中的关键作用，通过激活星状细胞和促进胶原沉积驱动纤维化进程，提示其作为抗纤维化治疗靶点。
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3. **文献名称**: *Galectin-3 Modulates T Cell Activity and Mediates Inflammatory Response*
**作者**: Liu FT, et al.
**摘要**: 研究发现重组Galectin-3通过结合T细胞表面糖蛋白调控Th1/Th2免疫平衡，参与慢性炎症及自身免疫疾病机制，为免疫调节提供了新方向。
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4. **文献名称**: *Recombinant Galectin-3 Induces Cancer Cell Adhesion and Metastasis*
**作者**: Raz A, et al.
**摘要**: 通过体外实验证明，重组Galectin-3蛋白促进肿瘤细胞与血管内皮细胞的黏附，增强转移能力，其机制与整合素信号通路激活相关。
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这些文献覆盖了Galectin-3在凋亡、纤维化、免疫及肿瘤转移中的多功能性研究，均为该领域的奠基性工作。
**Background of Recombinant Lgals3 Protein**
Lgals3. also known as galectin-3. is a multifunctional protein belonging to the galectin family, characterized by its affinity for β-galactoside-containing glycans. Encoded by the *LGALS3* gene in humans, it plays pivotal roles in cellular processes such as inflammation, immune regulation, cell adhesion, apoptosis, and intracellular signaling. Structurally, galectin-3 is unique among galectins due to its chimeric design: a C-terminal carbohydrate recognition domain (CRD) linked to an N-terminal proline-rich non-lectin domain, enabling multivalent interactions with ligands.
Recombinant Lgals3 protein is produced using biotechnological systems (e.g., *E. coli*, mammalian cells) to ensure high purity and activity for research and therapeutic applications. Its production often involves gene cloning, expression optimization, and purification via affinity chromatography. Recombinant galectin-3 retains the native protein's ability to bind glycoproteins, glycolipids, and extracellular matrix components, making it invaluable for studying its biological functions.
In research, recombinant Lgals3 is used to investigate its dual roles in health and disease. It acts as a mediator in fibrosis, cancer progression (promoting metastasis and angiogenesis), and chronic inflammation (e.g., atherosclerosis). Conversely, it also exhibits protective effects in acute injury models. Therapeutically, targeting galectin-3 has gained interest, with recombinant proteins or inhibitors being explored for treating fibrosis, heart failure, and cancer.
Despite its promise, galectin-3's context-dependent functions necessitate careful study. Recombinant Lgals3 remains a critical tool for dissecting molecular mechanisms and advancing therapeutic strategies.
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