纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | THYN1 |
Uniprot No | Q9P016 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-225aa |
氨基酸序列 | MSRPRKRLAG TSGSDKGLSG KRTKTENSGE ALAKVEDSNP QKTSATKNCL KNLSSHWLMK SEPESRLEKG VDVKFSIEDL KAQPKQTTCW DGVRNYQARN FLRAMKLGEE AFFYHSNCKE PGIAGLMKIV KEAYPDHTQF EKNNPHYDPS SKEDNPKWSM VDVQFVRMMK RFIPLAELKS YHQAHKATGG PLKNMVLFTR QRLSIQPLTQ EEFDFVLSLE EKEPS |
预测分子量 | 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THYN1重组蛋白的3条参考文献示例(内容为虚构,仅供格式参考):
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1. **文献名称**: "Cloning and Functional Characterization of Recombinant THYN1 Protein in Bacterial Expression Systems"
**作者**: Smith A, et al.
**摘要**: 本研究成功构建了THYN1基因的重组表达载体,并利用大肠杆菌系统高效表达可溶性THYN1蛋白。通过亲和层析纯化后,验证了其与DNA结合活性,为后续功能研究奠定基础。
2. **文献名称**: "Structural Insights into THYN1 Recombinant Protein by Cryo-EM and Its Role in Chromatin Remodeling"
**作者**: Johnson R, et al.
**摘要**: 通过冷冻电镜技术解析了重组THYN1蛋白的三维结构,发现其N端结构域与组蛋白H3特异性互作,揭示了THYN1在染色质重塑中的潜在分子机制。
3. **文献名称**: "THYN1 Recombinant Protein Attenuates Tumor Growth via Modulating p53 Signaling Pathway"
**作者**: Chen L, et al.
**摘要**: 在体外和体内实验中,重组THYN1蛋白通过激活p53依赖性凋亡通路显著抑制癌细胞增殖,提示其作为肿瘤治疗靶点的潜力。
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*注:以上文献及内容均为模拟生成,实际研究中需通过学术数据库(如PubMed、Web of Science)检索真实文献。*
**Background of THYN1 Recombinant Protein**
THYN1 (Thymocyte Nuclear Protein 1) is a protein encoded by the *THYN1* gene, which is conserved across eukaryotes and implicated in critical cellular processes. Initially identified in thymocytes, THYN1 localizes to the nucleus and is suggested to play roles in cell cycle regulation, DNA repair, and transcriptional control. Structurally, it contains conserved domains associated with nucleic acid binding, hinting at interactions with DNA or RNA. Though its precise molecular mechanisms remain under investigation, studies link THYN1 to maintaining genomic stability and modulating apoptosis, particularly in immune and cancer cells.
Recombinant THYN1 protein is engineered using expression systems like *E. coli* or mammalian cells, ensuring high purity and bioactivity for experimental use. Its production enables functional studies, such as elucidating interactions with partner proteins (e.g., transcription factors or chromatin remodelers) and mapping pathways involved in cellular stress responses. Dysregulation of THYN1 has been observed in certain cancers and autoimmune disorders, suggesting its potential as a therapeutic target or diagnostic biomarker.
Current research focuses on resolving THYN1’s 3D structure, post-translational modifications, and tissue-specific roles. Challenges include clarifying its dual functions in promoting survival or death under varying stress conditions. Recombinant THYN1 also serves as a tool for drug screening, antibody development, and CRISPR-based functional genomics. As interest grows in targeting nuclear proteins for disease intervention, THYN1 represents a promising yet underexplored candidate bridging basic cell biology and translational medicine. Further studies may unlock its utility in precision oncology and immune modulation.
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