Analytical Data
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Gene name
NUP205
- Application
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Alternative Names
NUP205；C7orf14；KIAA0225；Nuclear pore complex Protein Nup205
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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
Q92621
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Expression Region
全长
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AA Sequence
full
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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
NUP205, a member of the nucleoporins, is a crucial component of the nuclear pore complex (NPC), which plays a vital role in the transport of molecules between the nucleus and the cytoplasm. This protein is specifically involved in the selective transport of macromolecules, including proteins and RNA, thus maintaining cellular homeostasis and gene expression regulation. Recent studies have indicated that NUP205 may also have implications in various diseases, particularly in cancer, where alterations in nuclear transport can contribute to tumor progression and metastasis. The structural and functional characterization of NUP205 through recombinant protein technologies has been a significant focus in the field of molecular biology, aiming to understand its specific interactions within the NPC and its role in nucleocytoplasmic transport mechanisms. Furthermore, advancements in recombinant protein expression systems have enabled researchers to produce NUP205 in sufficient quantities for detailed biochemical assays and structural analyses, paving the way for potential therapeutic targets that could modulate nuclear transport pathways. Overall, the exploration of NUP205 and its functional properties remains a promising area of research with implications for understanding cellular transport mechanisms and their relevance in human diseases.
