Analytical Data
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Gene name
NUP107
- Application
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Alternative Names
NUP84; Nuclear pore complex protein Nup107
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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
Q8BH74
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Expression Region
Leu554~Thr784
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Molecular Weight
30kDa
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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
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Protein Description
NUP107, a key component of the nuclear pore complex (NPC), plays a critical role in nucleocytoplasmic transport and maintenance of nuclear structure. The NPC is a large, multisubunit structure that regulates the movement of molecules between the nucleus and the cytoplasm, and NUP107 is essential for the assembly and stability of this complex. Studies have indicated that NUP107 is not only involved in classical nuclear transport but also has implications in various cellular processes, including cell cycle regulation and signal transduction. Its dysregulation has been associated with several diseases, including cancer, where alterations in nuclear transport pathways can lead to uncontrolled cell proliferation and tumor progression. The recombinant expression of NUP107 has become a focus of research to better understand its functional roles and interactions within the NPC and to explore its potential as a therapeutic target. By using advanced techniques such as X-ray crystallography and cryo-electron microscopy, researchers aim to elucidate the structural characteristics of NUP107 and its interactions with other nucleoporins, thereby providing insights into the mechanisms that govern nucleocytoplasmic transport and their implications in health and disease. Such studies offer the prospect of developing novel strategies to modulate NUP107 function for therapeutic purposes, enhancing our understanding of cellular dynamics and pathogenesis at the molecular level.
