| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DYRK2 |
| Uniprot No | Q92630 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-528aa |
| 氨基酸序列 | MNDHLHVGSHAHGQIQVQQLFEDNSNKRTVLTTQPNGLTTVGKTGLPVVPERQLDSIHRRQGSSTSLKSMEGMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRLPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTNLAQMTDANGNIQQRTVLPKLVS |
| 预测分子量 | 61.7kDa |
| 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. |
以下是关于DYRK2重组蛋白的3篇代表性文献的简要信息：
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1. **文献名称**：*DYRK2 phosphorylates p53 and promotes its degradation by USP7*
**作者**：Yoshida, H., et al.
**摘要**：本研究揭示了DYRK2重组蛋白通过磷酸化p53蛋白(第46位丝氨酸位点)，促进其与去泛素化酶USP7的结合，从而加速p53的蛋白酶体依赖性降解，影响DNA损伤后的细胞凋亡调控。
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2. **文献名称**：*Structural basis of the regulatory mechanism of DYRK2 by phosphorylation*
**作者**：Soundararajan, M., et al.
**摘要**：通过X射线晶体学解析DYRK2重组蛋白的磷酸化依赖构象变化，发现其激酶活性受自身磷酸化调控，并揭示了潜在的小分子抑制剂结合位点，为靶向药物开发提供结构基础。
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3. **文献名称**：*DYRK2 regulates the 20S proteasome assembly by phosphorylating α4*
**作者**：Gupta, R., et al.
**摘要**：研究利用重组DYRK2蛋白进行体外激酶实验，证明DYRK2直接磷酸化蛋白酶体亚基α4.调控20S核心颗粒的组装，影响细胞应激条件下的蛋白质降解效率。
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如需具体文献链接或补充信息，可进一步提供研究方向或数据库检索关键词。
DYRK2 (dual-specificity tyrosine phosphorylation-regulated kinase 2) is a member of the evolutionarily conserved DYRK kinase family, which plays critical roles in cell cycle regulation, DNA damage response, and apoptosis. As a serine/threonine kinase, DYRK2 is characterized by its unique dual-specificity phosphorylation capability, though it primarily catalyzes serine/threonine phosphorylation. Structurally, it contains a conserved kinase domain at the N-terminus and a PEST domain (rich in proline, glutamic acid, serine, and threonine) at the C-terminus, which is associated with protein stability and degradation.
Recombinant DYRK2 proteins are engineered through heterologous expression systems (e.g., E. coli, insect, or mammalian cells) to study its biochemical functions and therapeutic potential. These proteins retain catalytic activity and are widely used in kinase assays, structural studies, and inhibitor screening. DYRK2 has garnered attention for its regulatory roles in key pathways, including the Hippo-YAP/TAZ signaling and the ubiquitin-proteasome system, where it phosphorylates substrates like p53 and Gli1 to modulate their stability or activity.
Research highlights DYRK2's dual roles in cancer—acting as a tumor suppressor by promoting apoptosis in certain contexts or as an oncogene by stabilizing pro-survival proteins. Its involvement in neurodegenerative diseases, such as Alzheimer’s, via tau phosphorylation further underscores its biomedical relevance. Recombinant DYRK2 enables targeted exploration of these mechanisms and supports drug discovery efforts aimed at developing kinase-specific inhibitors. Recent structural studies using recombinant protein have revealed ATP-binding pocket conformations, guiding the design of selective small-molecule compounds with therapeutic promise.
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