Analytical Data
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基因名
DDX39B
- Application
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别名
DDX39B; UAP56; DEAD(Asp-Glu-Ala-Asp)Box Polypeptide 39B; 56 kDa U2AF65-associated protein; HLA-B-associated transcript 1 protein; ATP-dependent RNA helicase p47
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q13838
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表达区间
Ser45~Asp199
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分子量
21kDa
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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
DDX39B, a member of the DEAD-box RNA helicase family, plays a pivotal role in various RNA processing events, including splicing, transport, and translation. Its critical involvement in these cellular processes makes it a significant focus of research, particularly in the context of cancer and other diseases. Dysregulation of RNA helicases like DDX39B has been linked to oncogenic processes, thereby implicating its potential as a therapeutic target. Recent studies have highlighted DDX39B's impact on the regulation of gene expression and its interaction with RNA-binding proteins, which are key players in the maintenance of cellular homeostasis. Moreover, the understanding of DDX39B's structure-function relationship has advanced through recombinant protein studies, facilitating insights into its mechanistic roles and regulatory networks. This groundwork lays the foundation for further exploration of DDX39B in disease pathways, with the hope that elucidating its function will lead to novel interventions in cancer treatment and other related disorders.
