Analytical Data
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Gene name
NPC
- Application
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Alternative Names
Niemann Pick type C2 protein homologcE1
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Species
Dog
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Source
Yeast
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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
Q28895
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Expression Region
22-149aa
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Molecular Weight
16 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
The study of NPC (Nuclear Pore Complex) recombinant proteins has gained significant attention in recent years due to the critical role NPCs play in cellular transport and nuclear regulation. NPCs are large protein complexes that span the nuclear envelope, facilitating the selective transport of molecules between the nucleus and cytoplasm. Understanding their structure and function is essential for unraveling the mechanisms of gene expression, cell signaling, and overall cellular homeostasis. Research into NPC recombinant proteins aims to elucidate the intricate architecture and dynamics of these complexes, which consist of multiple nucleoporins. Advances in molecular biology techniques, such as protein engineering and expression systems, have enabled scientists to produce and characterize NPC components more effectively. These studies not only enhance our knowledge of the basic biological processes but also have implications for various diseases, including cancer and neurodegenerative disorders, where nuclear transport is often disrupted. By creating model systems using recombinant NPC proteins, researchers hope to identify potential therapeutic targets and develop strategies for modulating nuclear transport pathways, paving the way for innovative treatments in the future.
