Analytical Data
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Gene name
NPS
- Application
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Alternative Names
NPS；Neuropeptide S
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0C0P6
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Expression Region
70-89aa
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AA Sequence
S FRNGVGTGMK KTSFQRAKS
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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
Nuclear pore complex (NPC) proteins, particularly nucleoporins (Nups), play crucial roles in nucleocytoplasmic transport, cellular regulation, and maintaining nuclear integrity. NPS, a specific type of Nup, has garnered attention due to its pivotal function in facilitating the selective transport of proteins and RNA between the nucleus and cytoplasm. As the understanding of cellular mechanisms deepens, researchers have recognized that abnormalities in NPS and other nucleoporins can lead to various diseases, including cancer and neurodegenerative disorders. The structural complexity and dynamic nature of the NPC present significant challenges for studying NPS; however, advances in techniques such as cryo-electron tomography and X-ray crystallography have shed light on its intricate architecture and mechanisms of function. Additionally, the reconstitution of NPS proteins in vitro has emerged as a powerful approach to unraveling their roles and interactions within the NPC. This research is not only fundamental for comprehending cellular transport systems but also holds potential therapeutic implications, as targeting NPS dysfunction may offer novel strategies for treating related diseases. Thus, understanding the biology and biophysics of NPS reconstituted proteins is of paramount importance in both basic and applied biomedical research, paving the way for future discoveries and innovations in cell biology.
