Analytical Data
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Gene name
NUP214
- Application
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Alternative Names
NUP214；CAIN；CAN；KIAA0023；Nuclear pore complex Protein Nup214
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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
P35658-1
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Expression Region
1-97aa
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AA Sequence
MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSLLAVSNKYGL VFAGGASGLQIFPTKNLLIQNKPGDDPNKIVDKVQGLLVPMKFPIHH
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Molecular Weight
36 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
NUP214 is a nucleoporina, a crucial component of the nuclear pore complex (NPC), which regulates the transport of macromolecules between the nucleus and the cytoplasm. The study of NUP214 has gained significant interest due to its implication in various cellular processes and diseases, particularly in relation to cancer and viral infections. Notably, NUP214 has been identified as a key player in the pathogenesis of acute leukemia, where its fusion with other genes leads to the production of oncoproteins that disrupt normal cellular functions. Furthermore, NUP214 has been shown to facilitate the nuclear entry of several viruses, such as HIV and retroviruses, highlighting its role in viral pathogenesis and potential as a therapeutic target. Recombination and expression studies of NUP214 allow researchers to investigate its structural and functional properties, providing insights into its role in nucleocytoplasmic transport mechanisms and its involvement in disease processes. Understanding the molecular dynamics of NUP214 could lead to the development of novel strategies for disease intervention, making it a focal point in both basic and applied biomedical research.
