Analytical Data
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Gene name
NUP35
- Application
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Alternative Names
MP44; NP44; Mitotic phosphoprotein 44; Nuclear pore complex protein Nup53
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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
Q8NFH5
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Expression Region
Thr132~Lys310
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Molecular Weight
26kDa
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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
NUP35 is a critical component of the nuclear pore complex (NPC), which facilitates the bidirectional transport of molecules between the nucleus and the cytoplasm, thereby playing a vital role in cellular function and gene regulation. Recent studies have highlighted the significance of nuclear transport in various biological processes, including cell division, gene expression, and response to stress. Mutations or dysregulation of nucleoporins, including NUP35, have been implicated in several diseases, including cancer and neurodegenerative disorders. The study of recombinant NUP35 protein has gained attention as it allows researchers to investigate the structural and functional properties of this nucleoporin in vitro. By producing NUP35 as a recombinant protein, scientists can explore its binding interactions with other nucleoporins and nucleocytoplasmic transport receptors, providing deeper insights into the molecular mechanisms governing nucleocytoplasmic transport. Furthermore, understanding the dynamics of NUP35 may aid in the development of targeted therapeutic strategies aimed at diseases associated with nuclear transport dysfunction. Overall, research on recombinant NUP35 protein is advancing our knowledge of nuclear dynamics and its implications in health and disease.
