Analytical Data
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Gene name
NFIB
- Application
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Alternative Names
NFI-RED; NFIB2; NFIB3; CCAAT-box-binding transcription factor; TGGCA-binding protein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00712
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Expression Region
Met1~Gln233
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Molecular Weight
57.0kDa
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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
NFIB (Nuclear Factor I B) is a transcription factor that plays a pivotal role in various biological processes, including cellular development, differentiation, and response to stress. Research into NFIB has gained momentum due to its implications in several diseases, particularly in cancer. Studies have shown that NFIB is aberrantly expressed in various tumor types, contributing to oncogenesis by promoting cell proliferation, survival, and migration. Additionally, NFIB interacts with other signaling pathways and transcription factors, influencing the tumor microenvironment and immune response. Given its involvement in these critical mechanisms, NFIB has emerged as a potential therapeutic target, prompting investigations into its structure, function, and regulatory networks. Understanding the molecular mechanisms of NFIB could lead to novel strategies for cancer treatment and shed light on its role in normal physiology and disease. Researchers are employing various techniques, including molecular biology, genomics, and bioinformatics, to unravel NFIB's complex regulatory roles and identify downstream targets that may provide insight into its therapeutic potential. The ongoing studies focus on defining the specific contexts in which NFIB acts, how its activity is regulated, and its interactions with other cellular components, which are crucial for developing targeted interventions in diseases characterized by NFIB dysregulation. This research not only expands our understanding of NFIB's biological functions but also enhances the potential for developing innovative treatment strategies for cancer and other NFIB-related disorders.
