Analytical Data
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Gene name
NFYB
- Application
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Alternative Names
NFYB；HAP3；Nuclear transcription factor Y subunit beta
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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
P25208
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Expression Region
1-207aa
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AA Sequence
MTMDGDSSTTDASQLGISADYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGAVTATDGLSEELTEEAFTNQLPAGLITTDGQQQNVMVYTTSYQQISGVQQIQFS
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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
Related Products
Protein Description
NFYB (Nuclear Factor Y subunit B) is a critical transcription factor involved in the regulation of gene expression in various biological processes, including cell cycle progression, differentiation, and stress responses. Its role in cellular functions has garnered significant interest due to its implications in developmental biology and disease states, including cancer. The NFYB protein forms a heterotrimeric complex with NFYA and NFYC, binding to specific promoter regions and driving the expression of target genes. Research has shown that aberrations in NFYB expression and function can contribute to tumorigenesis and other pathologies, making it a potential target for therapeutic interventions. The recombinant production of NFYB enables detailed studies of its structural and functional properties, facilitating the dissection of its mechanisms of action in cellular contexts. By creating purified NFYB protein through recombinant DNA technology, researchers can investigate its interactions with other proteins, analyze its role in transcriptional regulation, and assess how post-translational modifications affect its functions. Understanding NFYB's biology could lead to novel strategies for cancer therapy and the manipulation of cellular processes for therapeutic benefit. Thus, the study of NFYB recombinant protein is crucial for advancing our knowledge of its roles in health and disease, driving future innovations in clinical applications and molecular biology.
