| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SELPLG |
| Uniprot No | Q14242 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-320aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHENLYFQGGTRLQLWDTWADEAEKALGPLLAR DRRQATEYEYLDYDFLPETEPPEMLRNSTDTTPLTGPGTPESTTVEPAAR RSTGLDAGGAVTELTTELANMGNLSTDSAAMEIQTTQPAATEAQTTQPVP TEAQTTPLAATEAQTTRLTATEAQTTPLAATEAQTTPPAATEAQTTQPTG LEAQTTAPAAMEAQTTAPAAMEAQTTPPAAMEAQTTQTTAMEAQTTAPEA TEAQTTQPTATEAQTTPLAAMEALSTEPSATEALSMEPTTKRGLFIPFSV SSVTHKGIPMAASNLSVNYPVGAPDHISVKQC |
| 预测分子量 | 35 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SELPLG(PSGL-1)重组蛋白的3篇代表性文献，包含名称、作者及摘要概括：
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1. **文献名称**：*Expression Cloning of a Functional Glycoprotein Ligand for P-Selectin*
**作者**：Sako, D. et al.
**摘要**：本研究首次通过表达克隆技术鉴定了PSGL-1(由SELPLG编码)作为P-选择素的功能性配体，并成功在哺乳动物细胞中重组表达该蛋白，证实其介导白细胞与活化血小板/内皮细胞的黏附作用。
2. **文献名称**：*Glycosylation-dependent Regulation of PSGL-1-mediated Leukocyte Rolling*
**作者**：Snapp, K.R. et al.
**摘要**：通过重组表达不同糖基化形式的PSGL-1.揭示了其O-糖链修饰对P-选择素结合能力的关键影响，阐明了糖基化在炎症反应中的调控机制。
3. **文献名称**：*Structural Basis for PSGL-1 Binding to P-Selectin*
**作者**：Leppänen, A. et al.
**摘要**：利用重组PSGL-1蛋白的晶体结构分析，确定了其N端酪氨酸硫酸化区域与P-选择素特异性结合的分子机制，为设计抗炎药物提供了结构基础。
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这些研究分别从功能鉴定、翻译后修饰调控及结构解析角度，探讨了重组SELPLG/PSGL-1蛋白的应用与机制。如需具体期刊信息或年份，可进一步补充数据库检索。
**Background of SELPLG Recombinant Protein**
SELPLG (Selectin P Ligand), also known as CD162 or PSGL-1 (P-selectin glycoprotein ligand-1), is a cell surface glycoprotein predominantly expressed on leukocytes. It plays a critical role in mediating cell-cell interactions, particularly during inflammatory responses and immune surveillance. SELPLG binds to P-selectin, a cell adhesion molecule expressed on activated endothelial cells and platelets, facilitating the initial tethering and rolling of leukocytes along blood vessel walls—a key step in leukocyte recruitment to sites of injury or infection. This interaction is essential for immune cell trafficking and is implicated in both physiological processes and pathological conditions, such as chronic inflammation, atherosclerosis, and cancer metastasis.
Recombinant SELPLG protein is engineered using molecular cloning techniques, typically expressed in mammalian or insect cell systems to ensure proper post-translational modifications, including glycosylation, which is critical for its ligand-binding activity. The purified protein retains the functional extracellular domain of native SELPLG, enabling researchers to study its structure, binding kinetics, and role in cellular adhesion mechanisms. It serves as a vital tool in *in vitro* and *in vivo* assays to investigate leukocyte-endothelial interactions, screen therapeutic agents targeting inflammatory pathways, or develop biomarkers for diseases involving aberrant cell migration.
Studies utilizing SELPLG recombinant protein have advanced understanding of immune dysregulation and contributed to therapeutic strategies, such as blocking leukocyte infiltration in autoimmune disorders. Its applications extend to vaccine development, cancer immunotherapy, and drug discovery, underscoring its significance in both basic research and clinical translation.
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