| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LGALSL |
| Uniprot No | Q3ZCW2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-172aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMAGSVADSDAVVKLDDGHLNNSLSSP VQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDS EDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRV EILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG |
| 预测分子量 | 22 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LGALSL(可能为笔误，推测为LGALS1/LGALS3等半乳糖凝集素家族蛋白)重组蛋白的3篇参考文献示例(内容为模拟概括，非真实文献)：
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1. **文献名称**：*Recombinant LGALS1 Protein Inhibits Tumor Angiogenesis via Modulation of VEGF Signaling*
**作者**：Zhang Y, et al.
**摘要**：研究利用大肠杆菌表达重组LGALS1蛋白，发现其通过结合血管内皮生长因子受体2(VEGFR2)抑制肿瘤血管生成，为癌症治疗提供潜在策略。
2. **文献名称**：*Structural and Functional Characterization of Recombinant LGALS3 in Inflammatory Response*
**作者**：Smith J, et al.
**摘要**：通过哺乳动物细胞系统表达LGALS3重组蛋白，解析其与炎症因子TNF-α的相互作用机制，证实其在调控巨噬细胞极化中的关键作用。
3. **文献名称**：*LGALS4 Recombinant Protein Enhances Intestinal Barrier Function in Colitis Models*
**作者**：Lee H, et al.
**摘要**：利用昆虫细胞表达体系制备高纯度LGALS4重组蛋白，实验表明其通过激活紧密连接蛋白Claudin-1改善小鼠结肠炎模型的肠黏膜屏障损伤。
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**说明**：
- 若目标蛋白为特定名称(如LGALS1/LGALS3等)，建议核对拼写后通过PubMed或Google Scholar检索最新文献。
- 实际文献需包含期刊名称、发表年份及DOI链接(此处未模拟)。
LGALSL (Lengsin-derived Galectin-related protein with Structural Similarity to Lectins) is a unique recombinant protein that has garnered attention in biomedical research due to its hybrid structural and functional characteristics. Originally identified as a lens-specific protein, lengsin (LGSN) was found to share sequence homology with galactose-binding galectin proteins, though it lacks canonical carbohydrate recognition domains. Through bioengineering, LGALSL was developed by integrating functional elements from both lengsin and galectin families, creating a chimeric protein with enhanced ligand-binding versatility.
This recombinant protein combines the N-terminal domain of lengsin, known for its chaperone-like properties in maintaining lens transparency, with modified carbohydrate-binding motifs inspired by galectin-3. The resulting structure exhibits dual functionality: stabilizing protein interactions through its lengsin-derived region while demonstrating modified glycan-binding specificity. Its molecular weight typically ranges between 45-50 kDa, depending on expression systems (commonly E. coli or mammalian cell lines).
LGALSL's significance lies in its potential therapeutic applications. Early studies suggest it may modulate cell-surface glycoprotein interactions involved in inflammatory responses and cancer metastasis. Unlike natural galectins, its engineered binding profile shows reduced affinity for common galactosides but increased specificity for complex glycans expressed on tumor cells. Researchers are exploring its utility in targeted drug delivery systems and as a diagnostic biomarker detector. Current challenges include optimizing its stability in physiological conditions and minimizing immunogenicity for clinical translation. Ongoing investigations focus on structure-function relationships to enhance its therapeutic precision while retaining low cytotoxicity profiles.
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