Analytical Data
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Gene name
NUP155
- Application
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Alternative Names
N155; Nucleoporin 155kDa
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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
O75694
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Expression Region
Gln1154~Asn1379
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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
Related Products
Protein Description
NUP155, a member of the nucleoporins family, plays a crucial role in the structure and function of the nuclear pore complex (NPC), which is essential for nucleocytoplasmic transport. Research into NUP155 has gained momentum due to its implications in various biological processes and its potential involvement in diseases such as cancer and neurodegeneration. As a core component of the NPC, NUP155 is involved in the regulation of the nuclear transport of proteins and RNA, impacting gene expression, cell signaling, and overall cellular homeostasis. Recent studies have demonstrated that NUP155 not only facilitates the transport of specific macromolecules but also participates in chromatin organization and cell cycle regulation. The recombinant protein form of NUP155 provides a valuable tool for studying its functional properties, interactions, and structural characteristics. By producing NUP155 as a recombinant protein, researchers can utilize techniques such as crystallography and NMR spectroscopy to better understand its mechanistic roles within the NPC. Additionally, examining how mutations or alterations in NUP155 may contribute to disease pathways can reveal potential therapeutic targets. The exploration of NUP155 and its recombinant protein serves to deepen our understanding of nucleocytoplasmic transport and its broader implications in health and disease.
