Analytical Data
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Gene name
NFX1
- Application
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Alternative Names
NFX2; Nuclear transcription factor, X box-binding protein 1
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Species
Mouse
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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
B1AY10
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Expression Region
His859~Asp1114
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Molecular Weight
32kDa
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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
NFX1, or Nuclear Factor X 1, is a transcription factor that plays a critical role in the regulation of various genes, particularly those involved in the immune response and cellular stress response. Research into NFX1 has gained attention due to its involvement in the modulation of immune pathways and its potential implications in diseases such as cancer and viral infections. The protein is known to interact with other cellular components, influencing cellular processes such as proliferation, differentiation, and apoptosis. Recent studies have focused on the recombinant production of NFX1 proteins to better understand their structure-function relationships and regulatory mechanisms. By utilizing recombinant DNA technology, researchers can produce large quantities of NFX1 for biochemical assays, structural analysis, and functional studies. This approach enables the exploration of NFX1's role in cellular signaling pathways and its potential as a therapeutic target. Understanding the molecular dynamics of NFX1 and its downstream effects may provide new insights into strategies for modulating immune responses and developing novel treatments for related diseases.
