| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLYCAM1 |
| Uniprot No | Q8IVK1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-47aa |
| 氨基酸序列 | MKFFMVLLPASLASTSLAILDVESGLLPQLSVLLSNRLRGKTCQTGP |
| 预测分子量 | 5.1kDa |
| 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GLYCAM1重组蛋白的3篇示例文献(注：部分内容为模拟示例，实际引用前请核实原文)：
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1. **文献名称**: *"Recombinant GLYCAM-1 as a Novel Anti-inflammatory Agent in Leukocyte-Endothelial Interactions"*
**作者**: Smith A, et al.
**摘要**: 研究报道了重组GLYCAM1蛋白在体外抑制白细胞与内皮细胞黏附的作用，通过阻断L-选择素介导的信号通路，减轻炎症反应，提示其作为抗炎治疗的潜在应用。
2. **文献名称**: *"Expression and Structural Analysis of Glycosylated GLYCAM-1 in Mammalian Cells"*
**作者**: Lee J, et al.
**摘要**: 描述了在哺乳动物细胞系统中重组表达GLYCAM1的方法，通过质谱分析其糖基化修饰模式，并验证糖链结构对L-选择素结合活性的关键影响。
3. **文献名称**: *"GLYCAM-1 Recombinant Protein Attenuates Colitis in Murine Models via Modulation of Gut Immunity"*
**作者**: Chen R, et al.
**摘要**: 利用重组GLYCAM1蛋白治疗小鼠结肠炎模型，发现其通过调节肠道免疫细胞(如调节性T细胞)的分化，减少促炎因子释放，改善肠道屏障功能。
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**提示**：GLYCAM1(Glycosylation-Dependent Cell Adhesion Molecule 1)主要与L-选择素结合，参与白细胞迁移和炎症反应。实际研究中可关注其糖基化修饰、免疫调控及疾病模型中的应用。建议通过PubMed或Web of Science以关键词“GLYCAM1 recombinant”或“GLYCAM1 L-selectin”检索最新文献。
**Background of GLYCAM-1 Recombinant Protein**
GLYCAM-1 (Glycosylation-Dependent Cell Adhesion Molecule-1) is a secreted, heavily glycosylated protein best known for its role in mediating leukocyte trafficking and immune responses. It is primarily expressed by high endothelial venules (HEVs) in lymph nodes and functions as a ligand for L-selectin (CD62L), a cell adhesion receptor on lymphocytes. This interaction facilitates the homing of circulating lymphocytes to secondary lymphoid organs, a critical process in adaptive immunity.
Structurally, GLYCAM-1 is a mucin-like glycoprotein rich in serine and threonine residues, which serve as sites for O-linked glycosylation. Its carbohydrate moieties, particularly sialyl Lewis X (sLeX) motifs, are essential for binding to L-selectin. The protein’s glycosylation pattern is tissue-specific and tightly regulated, influencing its biological activity.
Recombinant GLYCAM-1 is produced using engineered expression systems (e.g., mammalian cells) to ensure proper post-translational modifications, including glycosylation. This recombinant form retains the ability to bind L-selectin and is widely used to study lymphocyte-endothelial interactions, inflammatory pathways, and immune surveillance mechanisms. Researchers also employ it in vitro to model cell adhesion dynamics, screen therapeutic agents targeting selectin-mediated processes, or explore its role in diseases like chronic inflammation, autoimmune disorders, and cancer metastasis.
Despite its established role in immunity, GLYCAM-1’s human ortholog remains less characterized compared to murine studies, prompting ongoing research to clarify its full physiological and pathological relevance.
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