Analytical Data
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基因名
DYRK2
- Application
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别名
DYRK2；Dual specificity tyrosine-phosphorylation-regulated kinase 2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q92630
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表达区间
1-528aa
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氨基酸序列
MNDHLHVGSHAHGQIQVQQLFEDNSNKRTVLTTQPNGLTTVGKTGLPVVPERQLDSIHRRQGSSTSLKSMEGMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRLPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTNLAQMTDANGNIQQRTVLPKLVS
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分子量
61.7kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
DYRK2 (Dual-specificity Tyrosine-phosphorylation Regulated Kinase 2) is a member of the DYRK family of kinases, known for its role in various cellular processes, including cell cycle regulation, neuronal development, and apoptosis. The interest in DYRK2 has surged due to its implications in cancer and neurodegenerative diseases, as dysregulation of its activity is associated with tumorigenesis and neuronal dysfunction. Research has demonstrated that DYRK2 can phosphorylate key substrates involved in these pathways, modulating their activity and influencing cell fate. The recombinant expression of DYRK2 has emerged as a crucial tool in understanding its biochemical properties, interaction network, and potential as a therapeutic target. By generating and characterizing DYRK2 recombinant proteins, researchers can elucidate the kinase’s functional mechanisms, investigate its substrate specificity, and explore the effects of post-translational modifications. Furthermore, recombinant DYRK2 can be utilized in high-throughput screening assays to identify small molecule inhibitors or activators, paving the way for novel cancer treatments and neuroprotective strategies. Overall, the study of DYRK2 through recombinant protein technology not only contributes to our understanding of its biological functions but also holds promise for advancing therapeutic approaches in diseases where DYRK2 plays a pivotal role.
