Analytical Data
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基因名
DYRK4
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简介
The DYRK4 protein may play a non-essential role in spermatogenesis, suggesting involvement in sperm cell development. Although specific functions and molecular mechanisms are unknown, its association with spermatogenesis suggests that it plays a role in complex pathways controlling male germ cell maturation. DYRK4 Protein, Human (sf9, GST) is the recombinant human-derived DYRK4 protein, expressed by sf9 insect cells , with GST tagged.
- Application
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别名
DYRK4; Dual specificity tyrosine-phosphorylation-regulated kinase 4
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种属
Human
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表达系统
Baculovirus
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标签
GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9NR20-1
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表达区间
P2-V520
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蛋白长度
Partial
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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
DYRK4 (Dual-specificity tyrosine phosphorylation-regulated kinase 4) is a member of the DYRK family of kinases, known for their roles in various cellular processes, including differentiation, proliferation, and stress responses. Research into DYRK4 has gained traction due to its implications in several diseases, particularly neurodegenerative conditions and cancers. It is uniquely characterized by its dual specificity for serine/threonine and tyrosine residues, which allows it to modulate multiple signaling pathways. Recent studies suggest that DYRK4 interacts with critical proteins involved in neuronal function and development, pointing to its potential as a therapeutic target. Furthermore, its dysregulation has been associated with aberrant cellular behaviors, highlighting the necessity for understanding its molecular mechanisms. Investigating DYRK4 recombinant proteins offers a valuable approach to elucidate its biological functions and regulatory roles within cells, paving the way for novel strategies in disease intervention. As research continues to unveil its complex interactions, DYRK4 stands out as a pivotal focus in the landscape of kinase biology and therapeutic development.
