Analytical Data
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Gene name
NIN
- Application
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Alternative Names
NIN；KIAA1565；Ninein
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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
Q8N4C6
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Expression Region
全长
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AA Sequence
full
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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
Nuclear Initiation Factor 1 (NIN) is a critical component in the regulation of nucleic acid metabolism and cellular responses to various stimuli, particularly in the context of oncogenesis and cellular stress. Research into NIN and its recombinant proteins has gained momentum due to its pivotal role in transcriptional regulation and its potential implications in cancer biology. Studies have shown that alterations in NIN expression can influence cell proliferation, differentiation, and survival, linking it to tumorigenic processes. Moreover, the recombinant expression of NIN provides a valuable tool for investigating its functional properties, interactions with other cellular components, and its mechanism of action in both normal and pathological states. The ability to produce NIN as a recombinant protein facilitates the exploration of its structural and functional characteristics, enabling researchers to elucidate its role in gene regulation and its potential as a therapeutic target. Recent advances in protein engineering and characterization techniques have further enhanced the understanding of NIN's conformational dynamics and interaction networks, paving the way for innovative approaches in cancer treatment and diagnostics. Overall, the study of NIN recombinant proteins holds promise for advancing our understanding of cellular mechanisms and developing novel interventions in cancer and other diseases influenced by dysregulated nucleic acid processes.
