Analytical Data
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Gene name
NFIA
- Application
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Alternative Names
NF-IA; NF1A; NFI-L; NF1-A; Nuclear Factor 1 A; 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
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q12857
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Expression Region
Met1~Glu143
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Molecular Weight
22kDa
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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
NFIA (Nuclear Factor I A) is a transcription factor that plays a crucial role in various biological processes, including cell differentiation, neural development, and tissue homeostasis. The study of NFIA has gained significant attention due to its involvement in developmental disorders and its potential links to cancer progression. Research has shown that NFIA is essential for the proper formation of certain tissues during embryogenesis, particularly in the central nervous system. Its ability to regulate gene expression by binding to specific DNA sequences makes NFIA a key player in gene regulatory networks. Moreover, dysregulation of NFIA has been implicated in various pathologies, including neurodevelopmental disorders, where aberrant NFIA function may disrupt normal brain development and contribute to cognitive deficits. Additionally, recent studies have suggested that NFIA might influence the tumor microenvironment, impacting cancer cell behavior and therapy resistance. As a result, understanding the structural and functional aspects of NFIA through protein reconstitution studies is critical for elucidating its mechanisms of action and therapeutic potential. By exploring NFIA’s protein interactions, post-translational modifications, and its role in modulating cellular pathways, researchers aim to uncover novel insights that could lead to targeted interventions for diseases associated with NFIA dysregulation, thus highlighting its significance in both developmental biology and clinical research.
