Analytical Data
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Gene name
NUP214
- Application
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Alternative Names
CAIN; CAN; N214; Nuclear Pore Complex Protein Nup214; CAN Protein,Putative Oncogene
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Species
Mouse
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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
Q80U93
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Expression Region
Ser601~Arg868
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Molecular Weight
37kDa
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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, a nucleoporin that plays a crucial role in the nuclear pore complex, is involved in various cellular processes including nucleocytoplasmic transport and maintaining nuclear integrity. Recent studies have highlighted the significance of NUP214 in different diseases, particularly its association with certain hematological malignancies, such as acute myeloid leukemia (AML) and T-cell acute lymphoblastic leukemia (T-ALL), where it often forms fusions with other genes, leading to dysregulation of essential cellular functions. The unique structural and functional properties of the NUP214 protein, especially its role in facilitating the transport of macromolecules across the nuclear envelope, have made it a target of intense investigation. Researchers are increasingly focused on the recombinant expression and characterization of NUP214 to better understand its functional mechanisms and interactions within the nuclear pore complex. This knowledge is vital for elucidating its contribution to leukemia pathogenesis and for the development of potential therapeutic strategies targeting NUP214-related pathways. The production of NUP214 as a recombinant protein allows for detailed biochemical studies, structural analyses, and the exploration of its function in cellular contexts. Ongoing research aims to unravel the intricate roles of NUP214 in nuclear transport dynamics and its implications in disease, paving the way for innovative approaches in treating NUP214-associated disorders.
