Analytical Data
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Gene name
NUP153
- Application
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Alternative Names
NUP153；Nuclear pore complex Protein Nup153
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49790
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Expression Region
657-880aa
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AA Sequence
KAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFKPVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECSVCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPG
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Molecular Weight
27.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
