| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRAME |
| Uniprot No | P78395 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-509aa |
| 氨基酸序列 | MERRRLWGSIQSRYISMSVWTSPRRLVELAGQSLLKDEALAIAALELLPRELFPPLFMAAFDGRHSQTLKAMVQAWPFTCLPLGVLMKGQHLHLETFKAVLDGLDVLLAQEVRPRRWKLQVLDLRKNSHQDFWTVWSGNRASLYSFPEPEAAQPMTKKRKVDGLSTEAEQPFIPVEVLVDLFLKEGACDELFSYLIEKVKRKKNVLRLCCKKLKIFAMPMQDIKMILKMVQLDSIEDLEVTCTWKLPTLAKFSPYLGQMINLRRLLLSHIHASSYISPEKEEQYIAQFTSQFLSLQCLQALYVDSLFFLRGRLDQLLRHVMNPLETLSITNCRLSEGDVMHLSQSPSVSQLSVLSLSGVMLTDVSPEPLQALLERASATLQDLVFDECGITDDQLLALLPSLSHCSQLTTLSFYGNSISISALQSLLQHLIGLSNLTHVLYPVPLESYEDIHGTLHLERLAYLHARLRELLCELGRPSMVWLSANPCPHCGDRTFYDPEPILCPCFMPN |
| 预测分子量 | 61.9kDa |
| 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3篇与PRAME重组蛋白相关的文献示例(注：以下为模拟虚构内容，实际文献需通过学术数据库查询)：
1. **《重组PRAME蛋白在黑色素瘤免疫治疗中的体外功能研究》**
作者：Smith A, et al.
摘要：研究利用大肠杆菌表达系统成功制备重组PRAME蛋白，证实其能有效激活患者外周血T细胞，诱导特异性免疫反应，为基于PRAME的肿瘤疫苗开发提供实验依据。
2. **《PRAME重组抗原在肺癌血清学诊断中的价值评估》**
作者：Zhang L, et al.
摘要：通过哺乳动物细胞表达系统获得高纯度PRAME重组蛋白，发现其在非小细胞肺癌患者血清中具有高特异性抗体识别率，提示其作为血清标志物的潜在诊断价值。
3. **《结构导向的PRAME重组蛋白表位修饰增强抗体结合能力》**
作者：Tanaka K, et al.
摘要：采用晶体结构分析指导PRAME重组蛋白的抗原表位改造，工程化后的重组蛋白对治疗性单克隆抗体的亲和力提升5倍，为优化免疫检测试剂提供新策略。
4. **《原核与真核系统表达PRAME重组蛋白的免疫原性比较》**
作者：Wang X, et al.
摘要：对比大肠杆菌和HEK293细胞表达的PRAME重组蛋白，发现真核系统产物因正确糖基化修饰表现出更强的树突状细胞活化能力，提示表达系统选择对治疗性抗原开发的重要性。
**Background of PRAME Recombinant Protein**
The **PRAME (Preferentially Expressed Antigen in Melanoma)** protein is a cancer/testis antigen (CTA) initially identified for its overexpression in melanoma and other malignancies, including lung, breast, and ovarian cancers. Normally, PRAME expression is restricted to immune-privileged tissues like the testis and ovary but is aberrantly activated in tumors, making it a promising target for immunotherapy and diagnostic applications. Its role in oncogenesis involves epigenetic regulation, apoptosis inhibition, and modulation of retinoic acid signaling, contributing to tumor proliferation and immune evasion.
**Recombinant PRAME protein** is engineered through molecular cloning, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells), followed by purification to ensure high specificity and functionality. This engineered protein retains key epitopes and structural motifs, enabling its use in antibody production, T-cell activation assays, and vaccine development. Researchers leverage recombinant PRAME to study its interaction with immune receptors, evaluate its immunogenicity, and design targeted therapies like CAR-T cells or peptide vaccines.
Clinically, PRAME serves as a biomarker for minimal residual disease monitoring and a prognostic indicator. Its tumor-specific expression minimizes off-target effects in therapeutic strategies, though challenges remain in addressing its low immunogenicity and heterogeneity across cancer types. Recent advances in recombinant protein engineering aim to enhance stability and immunostimulatory properties, bolstering its utility in next-generation cancer immunotherapies.
In summary, PRAME recombinant protein bridges translational research and clinical innovation, offering tools to dissect its biological mechanisms and develop precision oncology solutions.
×
