| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD15 |
| Uniprot No | Q01151 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-205aa |
| 氨基酸序列 | MSRGLQLLLLSCAYSLAPATPEVKVACSEDVDLPCTAPWDPQVPYTVSWVKLLEGGEERMETPQEDHLRGQHYHQKGQNGSFDAPNERPYSLKIRNTTSCNSGTYRCTLQDPDGQRNLSGKVILRVTGCPAQRKEETFKKYRAEIVLLLALVIFYLTLIIFTCKFARLQSIFPDFSKAGMERAFLPVTSPNKHLGLVTPHKTELV |
| 预测分子量 | 23 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CD15重组蛋白的模拟参考文献示例(仅供参考，非真实文献)：
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1. **文献名称**: *"Recombinant CD15 Glycoprotein Expression in CHO Cells and Its Role in Neutrophil Adhesion"*
**作者**: Zhang, L., et al.
**摘要**: 该研究报道了在CHO细胞中高效表达CD15重组糖蛋白的方法，并验证其与内皮选择素(E-selectin)的特异性结合，揭示了CD15在中性粒细胞炎症迁移中的分子机制。
2. **文献名称**: *"Structural Analysis of CD15 Antigen Using Recombinant Protein Crystallography"*
**作者**: Müller, R., & Schmidt, K.
**摘要**: 通过重组CD15蛋白的晶体结构解析，阐明了其Lewis X表位的三维构象，为开发靶向CD15的癌症免疫疗法提供了结构基础。
3. **文献名称**: *"CD15 Recombinant Protein as a Biomarker for Colorectal Cancer Diagnosis"*
**作者**: Tanaka, H., et al.
**摘要**: 研究利用重组CD15蛋白开发了一种新型ELISA检测方法，证实其在结直肠癌患者血清中的高表达水平，提示其作为肿瘤诊断标志物的潜力。
4. **文献名称**: *"Functional Characterization of Recombinant CD15 in Bacterial Pathogen Adhesion Studies"*
**作者**: Chen, J., & Wang, Y.
**摘要**: 该文献通过重组CD15蛋白模拟宿主细胞表面受体，揭示了某些病原体(如幽门螺杆菌)利用CD15介导宿主感染的分子途径。
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**注**：以上文献为模拟生成，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
CD15. also known as Lewis X antigen or SSEA-1 (Stage-Specific Embryonic Antigen-1), is a carbohydrate epitope primarily expressed on cell surface glycoproteins and glycolipids. Structurally, it consists of the trisaccharide Galβ1-4(Fucα1-3)GlcNAc, functioning as a terminal glycosylation modification. This glycosphingolipid plays critical roles in cell-cell recognition, adhesion, and signaling processes, particularly in immune responses and embryonic development.
In immunology, CD15 is prominently expressed on granulocytes, monocytes, and certain activated lymphocytes, serving as a biomarker for myeloid differentiation. It facilitates leukocyte extravasation by interacting with endothelial selectins during inflammation. CD15 overexpression has been observed in various cancers (e.g., Hodgkin lymphoma, colorectal carcinoma), where it contributes to metastasis and immune evasion, making it a potential therapeutic target.
Recombinant CD15 protein is artificially produced using expression systems (e.g., mammalian, insect cells) to preserve proper glycosylation patterns. This engineered protein enables researchers to study CD15-mediated biological processes without isolating it from native sources. Applications include:
1) Developing monoclonal antibodies for cancer diagnostics
2) Investigating leukocyte-endothelial interactions in inflammatory diseases
3) Exploring stem cell differentiation mechanisms
4) Screening carbohydrate-based inhibitors for therapeutic development
Recent studies highlight its utility in glycoengineering vaccines and CAR-T therapies targeting CD15-positive malignancies. Challenges remain in replicating complex glycosylation profiles during recombinant production, driving advancements in synthetic biology and glycoengineering techniques. As a research tool, recombinant CD15 continues to bridge gaps between glycobiology and clinical applications.
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