| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NFYA |
| Uniprot No | P23511-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-318aa |
| 氨基酸序列 | MEQYTANSNSSTEQIVVQAGQIQQQVQGQPLMVQVSGGQLITSTGQPIMV QAVPGGQGQTIMQVPVSGTQGLQQIQLVPPGQIQIQGGQAVQVQGQQGQT QQIIIQQPQTAVTAGQTQTQQQIAVQGQQVAQTAEGQTIVYQPVNADGTI LQQVTVPVSGMITIPAASLAGAQIVQTGANTNTTSSGQGTVTVTLPVAGN VVNSGGMVMMVPGAGSVPAIQRIPLPGAEMLEEEPLYVNAKQYNRILKRR QARAKLEAEGKIPKERRKYLHESRHRHAMARKRGEGGRFFSPKEKDSPHM QDPNQADEEAMTQIIRVS |
| 预测分子量 | 34 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NFYA重组蛋白的3篇参考文献，包含文献名称、作者及摘要概括：
1. **文献名称**：*"Recombinant NF-YA subunit synthesis and functional analysis of its DNA-binding domain"*
**作者**：Mantovani, R. et al.
**摘要**：该研究通过重组表达技术在大肠杆菌中纯化NFYA蛋白，并分析其DNA结合特性。结果表明，NFYA需与NFYB/NFYC亚基形成异源三聚体才能有效识别并结合靶基因启动子区的CCAAT框，揭示了其转录调控的分子基础。
2. **文献名称**：*"Structural insights into NF-YA reorganization upon DNA binding"*
**作者**：Nardini, M. et al.
**摘要**：利用X射线晶体学解析了重组NFYA蛋白与DNA复合物的三维结构，发现NFYA的α螺旋结构域在结合DNA时发生构象变化，阐明了其通过保守氨基酸残基与CCAAT框特异性互作的机制。
3. **文献名称**：*"NFYA dysregulation in cancer: Recombinant protein-based functional studies"*
**作者**：Dolfini, D. et al.
**摘要**：通过重组NFYA蛋白的体外功能实验，证明其在多种癌细胞中异常高表达，并通过调控细胞周期相关基因(如CDK1、Cyclin B)促进肿瘤增殖，为靶向NFYA的癌症治疗提供了依据。
以上文献涵盖了NFYA重组蛋白的结构、DNA结合机制及病理功能研究，可供进一步参考。
**Background of NFYA Recombinant Protein**
The Nuclear Transcription Factor Y subunit A (NFYA) is a critical component of the NF-Y heterotrimeric transcription factor complex, which also includes NFYB and NFYC. NF-Y binds to the CCAAT box, a DNA motif found in the promoter regions of numerous eukaryotic genes, regulating their expression. NFYA plays a central role in this complex by mediating sequence-specific DNA binding through its conserved N-terminal domain, while its C-terminal region facilitates interactions with NFYB/NFYC to stabilize the trimeric structure. This complex is essential for modulating genes involved in cell cycle progression, apoptosis, stress responses, and differentiation, making NFYA a pivotal player in cellular homeostasis and disease pathways.
Recombinant NFYA protein is typically produced using *in vitro* expression systems, such as *E. coli* or mammalian cell cultures, followed by purification via affinity chromatography (e.g., His-tag or GST-tag systems). Its recombinant form enables precise biochemical and functional studies, including analyses of DNA-protein interactions, transcriptional regulation mechanisms, and structural characterization. Researchers utilize NFYA recombinant protein to investigate its role in diseases like cancer, where dysregulated NF-Y activity is linked to tumorigenesis, or in metabolic disorders. Additionally, it serves as a tool for screening small-molecule inhibitors or activators targeting NF-Y-dependent pathways.
Quality control measures, such as SDS-PAGE, Western blotting, and functional assays (e.g., electrophoretic mobility shift assays), ensure the protein’s purity and activity. By providing a standardized, high-purity reagent, recombinant NFYA accelerates research into transcriptional networks and therapeutic strategies aimed at modulating NF-Y function.
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