Analytical Data
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基因名
NUP153
- Application
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别名
NUP153；Nuclear pore complex Protein Nup153
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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
P49790
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表达区间
657-880aa
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氨基酸序列
KAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFKPVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECSVCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPG
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分子量
27.3 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
NUP153, a nucleoporins protein, is a crucial component of the nuclear pore complex (NPC), which facilitates the transport of molecules between the nucleus and cytoplasm in eukaryotic cells. Research on NUP153 has garnered attention due to its significant roles in various cellular processes, including gene expression regulation, nuclear transport, and the maintenance of genomic stability. Abnormalities in NUP153 expression or function have been linked to several diseases, including cancer and viral infections, where it plays a role in the life cycle of certain viruses by aiding their nuclear entry. Furthermore, NUP153 has been shown to interact with various nucleic acids and proteins, highlighting its involvement in RNA processing and gene regulation. The study of recombinant NUP153 protein offers insights into its structural and functional properties, enabling researchers to explore its mechanisms of action and impacts on cellular function. This understanding can potentially lead to novel therapeutic strategies aimed at manipulating NUP153 activity in disease contexts, making it a significant focus of current research in cell biology and molecular medicine. As such, investigating recombinant NUP153 protein provides valuable information about its biological roles, interactions, and applications in biomedical research.
