Analytical Data
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基因名
DYRK3
- Application
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别名
DYRK3；Dual specificity tyrosine-phosphorylation-regulated kinase 3
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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
O43781-2
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表达区间
63-568aa
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氨基酸序列
MKVEQLFQEFGNRKSNTIQSDGISDSEKCSPTVSQGKSSDCLNTVKSNSS SKAPKVVPLTPEQALKQYKHHLTAYEKLEIINYPEIYFVGPNAKKRHGVI GGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLR QYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRN HVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSILQSLDALHKNKII HCDLKPENILLKHHGRSSTKVIDFGSSCFEYQKLYTYIQSRFYRAPEIIL GSRYSTPIDIWSFGCILAELLTGQPLFPGEDEGDQLACMMELLGMPPPKL LEQSKRAKYFINSKGIPRYCSVTTQADGRVVLVGGRSRRGKKRGPPGSKD WGTALKGCDDYLFIEFLKRCLHWDPSARLTPAQALRHPWISKSVPRPLTT IDKVSGKRVVNPASAFQGLGSKLPPVVGIANKLKANLMSETNGSIPLCSV LPKLIS
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分子量
95 kDa
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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
DYRK3 (Dual-specificity tyrosine-phosphorylation-regulated kinase 3) is a member of the DYRK family of kinases, which are known for their roles in various cellular processes, including cell proliferation, differentiation, and apoptosis. The study of DYRK3 has garnered attention due to its potential involvement in neurodevelopmental disorders and cancer, where aberrant regulation of kinase activity may contribute to disease pathogenesis. Research indicates that DYRK3 is implicated in the phosphorylation of key substrates that regulate signaling pathways critical for maintaining cellular homeostasis. Moreover, its unique dual-specificity allows it to phosphorylate both serine/threonine and tyrosine residues, adding complexity to its functional role in cellular signaling. Given the increasing evidence linking DYRK3 to various pathologies, the development of recombinant DYRK3 proteins has become essential for investigating their biochemical properties, substrate specificity, and potential therapeutic applications. Recombining DYRK3 could facilitate the elucidation of its mechanism of action, providing insights into its regulation and the discovery of novel inhibitors. As the understanding of DYRK3 continues to evolve, it holds promise as a target for therapeutic intervention in diseases associated with its dysregulation, highlighting the importance of characterizing this kinase through recombinant protein studies.
