| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CK2 |
| Uniprot No | P19784 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 8-350aa |
| 氨基酸序列 | RARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSAN |
| 预测分子量 | 56.7kDa |
| 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篇关于CK2(酪蛋白激酶2)重组蛋白的参考文献摘要：
1. **文献名称**：*Expression and purification of the recombinant human protein kinase CK2 subunits α and β*
**作者**：Grankowski N, et al.
**摘要**：该研究描述人源CK2激酶α和β亚基在大肠杆菌中的重组表达及纯化方法，利用亲和层析技术获得高活性蛋白，并验证其体外激酶活性。
2. **文献名称**：*Structural insights into the regulation of protein kinase CK2 by the regulatory subunit CK2β*
**作者**：Niefind K, et al.
**摘要**：通过X射线晶体学解析CK2全酶(α2β2复合物)的三维结构，揭示β亚基对α催化亚基活性调控的分子机制，为靶向CK2的药物设计提供依据。
3. **文献名称**：*Functional characterization of recombinant CK2 holoenzyme in cancer cell signaling*
**作者**：Ruzzene M, et al.
**摘要**：利用昆虫细胞表达系统重组生产CK2全酶，研究其在肿瘤细胞中通过磷酸化p53、Akt等关键蛋白调控增殖和凋亡的分子通路。
(注：以上文献为示例，实际引用时请核对原始文献信息及期刊名称。)
**Background of CK2 Recombinant Protein**
Casein kinase 2 (CK2), also known as protein kinase CK2. is a highly conserved and ubiquitously expressed serine/threonine kinase involved in diverse cellular processes, including cell growth, proliferation, apoptosis, and DNA repair. Structurally, CK2 typically exists as a tetrameric complex composed of two catalytic subunits (α or α') and two regulatory β subunits, though recombinant forms often focus on the catalytic α subunit for functional studies.
The development of recombinant CK2 proteins emerged to overcome limitations in isolating the native enzyme from biological sources, which is labor-intensive and yields low quantities. Using recombinant DNA technology, CK2 subunits are cloned and expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., insect or mammalian cells) to produce active, purified kinase. Recombinant CK2 retains enzymatic activity and substrate specificity, enabling precise investigation of its biological roles and interactions.
CK2 is constitutively active and participates in numerous signaling pathways by phosphorylating over 300 substrates, including transcription factors, tumor suppressors, and viral proteins. Its dysregulation is linked to cancers, neurodegenerative diseases, and viral infections, making it a therapeutic target. Recombinant CK2 facilitates drug discovery by serving as a tool for high-throughput screening of inhibitors.
Studies using recombinant CK2 have elucidated its regulatory mechanisms, such as the β subunit's role in stabilizing the catalytic subunit and modulating substrate recognition. Additionally, engineered mutants (e.g., kinase-dead variants) help dissect CK2's functional domains.
In summary, recombinant CK2 proteins provide a standardized, scalable resource for biochemical, structural, and pharmacological research, advancing our understanding of CK2's multifaceted roles in health and disease.
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