Analytical Data
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Gene name
NFYB
- Application
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Alternative Names
CAAT box DNA-binding protein subunit B Nuclear transcription factor Y subunit B
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P25208
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Expression Region
1-207aa
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Molecular Weight
49.8 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
NFYB, or Nuclear Factor Y subunit B, is a transcription factor that plays a pivotal role in regulating gene expression in response to various environmental stimuli and developmental cues. It is part of a heterotrimeric complex comprised of NFYA, NFYB, and NFYC, which binds to specific DNA sequences known as CCAAT boxes located in the promoters of target genes. Research has increasingly highlighted NFYB's involvement in crucial biological processes such as cell cycle regulation, apoptosis, tissue differentiation, and responses to stressors like hypoxia or nutrient deprivation. Dysregulation of NFYB has been implicated in several pathologies, including cancer, where it can influence the proliferation and survival of tumor cells. This makes NFYB an attractive target for therapeutic interventions. Additionally, studies have shown that NFYB interacts with various signaling pathways, suggesting its potential role in mediating complex cellular responses. Given its significance in both fundamental physiology and disease states, ongoing research seeks to elucidate the precise mechanisms governing NFYB's function, its interactions with other cellular molecules, and its potential as a biomarker or therapeutic target in regenerative medicine and oncology. Understanding NFYB's multifaceted roles will not only enhance the fundamental knowledge of gene regulation but could also lead to innovative strategies for manipulating gene expression in therapeutic contexts.
