纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SART3 |
Uniprot No | Q15020 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 600-900aa |
氨基酸序列 | QRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPKVLHDSSKDSITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVDKSKNPDFKVFRYSTSLEKHKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNPPQRKVPEKPETRKAPGGPMLLP |
预测分子量 | 35.8 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SART3重组蛋白的3篇参考文献,按研究领域分类概括:
1. **《Identification of SART3-derived peptides capable of inducing HLA-A24-restricted cytotoxic T lymphocytes》**
- **作者**: Shichijo S, et al.
- **摘要**: 研究筛选了SART3抗原中能够激活HLA-A24限制性T细胞的表位肽,证明重组SART3蛋白在体外可诱导特异性T细胞杀伤肿瘤细胞,为癌症疫苗开发提供依据。
2. **《SART3. a novel squamous cell carcinoma antigen, promotes deubiquitination of spliceosomal snRNP proteins》**
- **作者**: Harada Y, et al.
- **摘要**: 揭示SART3通过调控剪接体小核RNP蛋白的去泛素化功能参与RNA剪接,其重组蛋白被用于验证其在肿瘤细胞异常剪接中的作用机制。
3. **《Induction of cellular immune responses to SART3-derived peptides in phase I clinical trial for head and neck cancer》**
- **作者**: Kawaguchi Y, et al.
- **摘要**: 基于SART3重组蛋白设计的多肽疫苗在头颈癌患者I期临床试验中显示出安全性,并能诱导特异性T细胞免疫应答,提示其潜在治疗价值。
**备注**:SART3作为肿瘤相关抗原,研究多聚焦于其免疫治疗应用(如疫苗靶点)及在RNA剪接中的促癌机制。如需全文链接或补充年份/期刊信息,可进一步说明。
**Background of SART3 Recombinant Protein**
SART3 (Squamous Cell Carcinoma Antigen Recognized by T-cells 3) is a multifunctional protein encoded by the *SART3* gene in humans, located on chromosome 12. Initially identified as a tumor-associated antigen, it is overexpressed in various cancers, including squamous cell carcinomas, and has been explored as a target for immunotherapy due to its immunogenic epitopes recognized by cytotoxic T-cells.
Structurally, SART3 contains two RNA recognition motifs (RRMs) and a proline-rich domain, enabling interactions with RNA and proteins. It plays dual roles in cellular processes:
1. **RNA Splicing Regulation**: As a component of the U4/U6.U5 tri-snRNP complex, SART3 is critical for pre-mRNA splicing by stabilizing U6 snRNA and facilitating spliceosome assembly.
2. **Telomerase Activity Modulation**: It interacts with telomerase reverse transcriptase (TERT), influencing telomere maintenance in cancer cells, thereby promoting proliferation and survival.
The recombinant SART3 protein, produced via genetic engineering in systems like *E. coli* or mammalian cells, retains these functional domains. It serves as a vital tool for studying RNA metabolism, spliceosome dynamics, and telomerase-related oncogenesis. In translational research, recombinant SART3 is utilized to develop cancer vaccines, T-cell therapies, and diagnostic assays, leveraging its antigenic properties and mechanistic roles in malignancy. Its dual functionality and cancer-specific expression make it a compelling candidate for both basic research and therapeutic innovation.
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