Analytical Data
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Gene name
NUP210
- Application
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Alternative Names
Nuclear envelope pore membrane protein POM 210 ;POM210Nucleoporin Nup210Pore membrane protein of 210KDA
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TEM1
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Expression Region
28-238aa
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Molecular Weight
27.6 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
NUP210, a nucleoporin that is part of the nuclear pore complex, plays a crucial role in nucleocytoplasmic transport, influencing the shuttling of proteins and RNA between the nucleus and the cytoplasm. Its unique structure and long cytoplasmic domain suggest that NUP210 may be involved in various cellular processes beyond mere transport, including gene expression regulation and response to cellular stress. Recent studies have highlighted its potential implications in cancer biology, as aberrations in nuclear transport mechanisms can lead to tumorigenesis. Furthermore, NUP210 has been implicated in certain viral infections that hijack the nuclear transport machinery for their replication, making it a target of interest for therapeutic strategies. To delve deeper into the functional properties of NUP210, researchers have turned to its recombinant protein for various assays, aiming to elucidate its structural and functional characteristics. Recombinant NUP210 can provide insights into its interactions with other nucleoporins and cellular factors, as well as its role in the nuclear pore complex assembly. Overall, the study of recombinant NUP210 is critical for understanding its multifaceted functions and potential therapeutic applications in diseases associated with dysregulated nucleocytoplasmic transport.
