Analytical Data
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Gene name
NSS
- Application
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Alternative Names
NSS；NAK；Serine/threonine-Protein kinase TBK1
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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
P12792
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Expression Region
1-267aa
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AA Sequence
MINNNMMNSQYMFDYPAINIDVRCHRLLSSVSYVAYNKFHTHDVSTYEHCEIPLEKLRLGFGRRNSLADFYSLGELPASWGPACYFSSVKPMMYTFQGMASDLSRFDLTSFSRKGLPNVLKALSWPLGIPDCEIFSICSDRFVRGLQTRDQLMSYILRMGDSHSLDECIVQAHKKILQEARRLGLSDEHYNGYDLFREIGSLVCLRLINAEPFDTASSGEALDVRTVIRSYRASDPSTGLTEYGNSLWTPIHSHVDENDESSSDSDF
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Molecular Weight
37.8 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
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Protein Description
NSS (Non-Structural Protein) restructuring proteins play a critical role in various biological processes, including viral replication, cellular signaling, and structural integrity. Researchers have become increasingly interested in these proteins due to their significance in understanding the mechanisms of viral infections and host-pathogen interactions. NSS proteins are often involved in the remodeling of cellular environments to facilitate processes such as viral assembly and release, making them essential targets for antiviral drug development. Additionally, studies have shown that NSS proteins can contribute to oncogenesis in cancer cells, highlighting their potential as biomarkers for cancer diagnosis and therapy. The ability of NSS proteins to undergo conformational changes in response to various stimuli is another area of active research, as these changes can influence their interactions and functional outcomes. By elucidating the structural and functional dynamics of NSS proteins, scientists aim to develop innovative therapeutic strategies to combat viral infections and associated diseases, thereby enhancing our understanding of disease mechanisms and improving clinical outcomes. The ongoing research into NSS restructuring proteins not only sheds light on fundamental biological processes but also offers promising avenues for therapeutic intervention in both virology and oncology.
