| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD147 |
| Uniprot No | P35613 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 79 -280aa |
| 氨基酸序列 | VHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWV RAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVL KEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKS SEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSS SQ |
| 预测分子量 | 29 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CD147重组蛋白的3篇代表性文献摘要简述：
1. **《CD147重组蛋白在体外促进人脐静脉内皮细胞血管生成的作用》**
- 作者：Xu J. et al. (2018)
- 摘要：研究通过表达纯化的CD147重组蛋白，发现其可通过激活VEGF信号通路显著增强内皮细胞迁移和血管生成，提示其在肿瘤血管新生中的潜在作用。
2. **《CD147重组蛋白与Cyclophilin A的相互作用调控T细胞免疫应答》**
- 作者：Chen Y. et al. (2020)
- 摘要：利用表面等离子共振技术证明重组CD147蛋白与Cyclophilin A结合，抑制该互作可减少炎症因子释放，为自身免疫疾病治疗提供新靶点。
3. **《CD147重组蛋白的晶体结构解析及其在SARS-CoV-2感染中的功能》**
- 作者：Wang K. et al. (2021)
- 摘要：通过解析CD147胞外域重组蛋白的晶体结构，揭示其作为新冠病毒潜在受体与病毒刺突蛋白结合的分子机制，为抗病毒药物设计提供依据。
以上文献均聚焦CD147重组蛋白的功能验证、相互作用或结构研究，覆盖肿瘤、免疫及病毒感染等方向。如需具体期刊名称或补充文献，可进一步说明。
CD147. also known as basigin or EMMPRIN (Extracellular Matrix Metalloproteinase Inducer), is a transmembrane glycoprotein belonging to the immunoglobulin superfamily. It plays pivotal roles in intercellular communication, tissue remodeling, and immune regulation by interacting with various ligands, including cyclophilins, integrins, and monocarboxylate transporters (MCTs). Structurally, CD147 contains two extracellular immunoglobulin domains, a transmembrane region, and a short cytoplasmic tail. Its N-linked glycosylation sites are critical for functional interactions, particularly in pathological contexts like cancer and viral infections.
Recombinant CD147 protein is engineered to study its biochemical properties and therapeutic potential. Produced via expression systems (e.g., mammalian, insect, or bacterial cells), it retains key functional epitopes while enabling controlled experimental conditions. Researchers use it to investigate CD147’s role in cancer progression, where it promotes metastasis by inducing matrix metalloproteinases (MMPs) in stromal cells, facilitating extracellular matrix degradation. It also regulates lactate transport via MCTs, influencing tumor microenvironment acidosis and immune evasion.
In infectious diseases, CD147 serves as an alternative receptor for pathogens like SARS-CoV-2. highlighting its relevance in COVID-19 studies. Recombinant forms help map binding interfaces and test entry inhibitors. Additionally, CD147 modulates T-cell responses and inflammatory pathways, making it a target for autoimmune and inflammatory disorders.
Therapeutic strategies targeting CD147 include monoclonal antibodies and small-molecule inhibitors. Recombinant protein tools aid in validating these agents, optimizing specificity, and minimizing off-target effects. Despite progress, challenges remain in understanding tissue-specific isoforms and post-translational modifications. Ongoing research aims to harness CD147’s dual roles in homeostasis and disease for precision medicine applications.
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