| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CEBPZ |
| Uniprot No | Q03701 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1054aa |
| 氨基酸序列 | MAAVKEPLEFHAKRPWRPEEAVEDPDEEDEDNTSEAENGFSLEEVLRLGGTKQDYLMLATLDENEEVIDGGKKGAIDDLQQGELEAFIQNLNLAKYTKASLVEEDEPAEKENSSKKEVKIPKINNKNTAESQRTSVNKVKNKNRPEPHSDENGSTTPKVKKDKQNIFEFFERQTLLLRPGGKWYDLEYSNEYSLKPQPQDVVSKYKTLAQKLYQHEINLFKSKTNSQKGASSTWMKAIVSSGTLGDRMAAMILLIQDDAVHTLQFVETLVNLVKKKGSKQQCLMALDTFKELLITDLLPDNRKLRIFSQRPFDKLEQLSSGNKDSRDRRLILWYFEHQLKHLVAEFVQVLETLSHDTLVTTKTRALTVAHELLCNKPEEEKALLVQVVNKLGDPQNRIATKASHLLETLLCKHPNMKGVVSGEVERLLFRSNISSKAQYYAICFLNQMALSHEESELANKLITVYFCFFRTCVKKKDVESKMLSALLTGVNRAYPYSQTGDDKVREQIDTLFKVLHIVNFNTSVQALMLLFQVMNSQQTISDRYYTALYRKMLDPGLMTCSKQAMFLNLVYKSLKADIVLRRVKAFVKRLLQVTCQQMPPFICGALYLVSEILKAKPGLRSQLDDHPESDDEENFIDANDDEDMEKFTDADKETEIVKKLETEETVPETDVETKKPEVASWVHFDNLKGGKQLNKYDPFSRNPLFCGAENTSLWELKKLSVHFHPSVALFAKTILQGNYIQYSGDPLQDFTLMRFLDRFVYRNPKPHKGKENTDSVVMQPKRKHFIKDIRHLPVNSKEFLAKEESQIPVDEVFFHRYYKKVAVKEKQKRDADEESIEDVDDEEFEELIDTFEDDNCFSSGKDDMDFAGNVKKRTKGAKDNTLDEDSEGSDDELGNLDDDEVSLGSMDDEEFAEVDEDGGTFMDVLDDESESVPELEVHSKVSTKKSKRKGTDDFDFAGSFQGPRKKKRNLNDSSLFVSAEEFGHLLDENMGSKFDNIGMNAMANKDNASLKQLRWEAERDDWLHNRDAKSIIKKKKHFKKKRIKTTQKTKKQRK |
| 分子量 | 120 KDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人CEBPZ蛋白的3-4篇模拟文献示例(基于研究领域常见方向整理，非真实文献)：
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1. **文献名称**: "Crystal Structure of Recombinant Human CEBPZ Reveals DNA-Binding Specificity"
**作者**: Thompson, L. et al.
**摘要**: 通过X射线晶体学解析了重组人CEBPZ蛋白的DNA结合域结构，揭示了其与特定CCAAT基序结合的分子机制，并发现磷酸化修饰影响其与染色质的结合能力。
2. **文献名称**: "Recombinant CEBPZ Enhances Ribosomal RNA Transcription via Interaction with RNA Polymerase I"
**作者**: Watanabe, K. et al.
**摘要**: 研究利用重组CEBPZ蛋白进行体外结合实验，证实其直接结合RNA聚合酶I复合物，调控核糖体RNA的转录活性，揭示了CEBPZ在细胞增殖中的新功能。
3. **文献名称**: "Functional Analysis of CEBPZ Isoforms Expressed in Mammalian Cells"
**作者**: Müller, S. et al.
**摘要**: 通过重组表达两种人源CEBPZ剪接变体，发现不同异构体在亚细胞定位及靶基因激活能力上的差异，为疾病相关突变研究提供了实验依据。
4. **文献名称**: "CEBPZ Knockdown and Recombinant Protein Rescue in Hematopoietic Stem Cells"
**作者**: Chen, H. et al.
**摘要**: 利用重组CEBPZ蛋白回补实验，证明其在造血干细胞分化中通过调控表观遗传修饰因子维持干细胞自我更新能力的必要性。
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**注**: 以上文献为领域方向模拟示例，实际引用时需检索真实数据库(如PubMed、Web of Science)获取原文信息。CEBPZ(CCAAT enhancer-binding protein zeta)的研究多聚焦于转录调控、癌症及干细胞分化等领域，重组蛋白技术常应用于其相互作用及功能验证实验。
C/EBPZ (CCAAT enhancer-binding protein zeta), also known as CEBPZOS or CHD4-associated protein, is a multifunctional nuclear protein implicated in transcriptional regulation and chromatin remodeling. It belongs to the CCAAT-binding protein family, which recognizes conserved CCAAT motifs in gene promoters to modulate RNA polymerase II-mediated transcription. C/EBPZ interacts with chromatin-modifying complexes, including the NuRD (Nucleosome Remodeling and Deacetylase) complex and histone methyltransferases like G9a, influencing histone modification patterns (e.g., H3K9 methylation) and chromatin accessibility. This protein plays roles in cellular processes such as cell cycle progression, differentiation, and apoptosis.
Studies highlight its dual functionality: it can act as a transcriptional activator or repressor depending on binding partners and cellular context. For instance, C/EBPZ is essential for ribosomal RNA (rRNA) synthesis by regulating RNA polymerase I activity, linking it to ribosome biogenesis. Dysregulation of C/EBPZ has been associated with cancers, where it may either promote tumorigenesis by enhancing oncogene expression or suppress cancer progression via apoptosis induction.
Recombinant human C/EBPZ protein, typically produced in *E. coli* or mammalian expression systems, retains DNA-binding and protein-interaction capabilities. It is widely used to study transcriptional mechanisms, screen small-molecule inhibitors, and explore its therapeutic potential. Research continues to elucidate its context-dependent roles and validate its utility as a diagnostic or therapeutic target.
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