Analytical Data
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Gene name
HNF4a
- Application
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Alternative Names
HNF4; HNF4a7; HNF4a8; HNF4a9; MODY; MODY1; NR2A1; NR2A21; TCF; TCF14; Nuclear Receptor Subfamily 2,Group A,Member 1; Transcription factor 14
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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
P41235
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Expression Region
Gln131~Ser330
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Molecular Weight
27kDa
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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
HNF4α (Hepatocyte Nuclear Factor 4 Alpha) is a key transcription factor primarily expressed in the liver, pancreas, and intestine, playing a crucial role in regulating metabolic pathways and maintaining glucose homeostasis. Abnormalities in HNF4α expression or function are associated with various metabolic disorders, including maturity-onset diabetes of the young (MODY) and non-alcoholic fatty liver disease (NAFLD). Recent studies have highlighted HNF4α as a critical player in liver development, lipid metabolism, and insulin signaling, thus making it a potential therapeutic target for diabetes and other metabolic diseases. The generation of recombinant HNF4α proteins allows researchers to explore its biochemical properties, regulatory mechanisms, and interactions with other proteins, providing insights into its role in disease. Utilizing techniques such as bacterial expression systems and mammalian cell culture, scientists can investigate the structure-function relationship of HNF4α, its DNA-binding capability, and its effect on target gene expression. Understanding the functional dynamics of HNF4α through recombinant protein studies can aid in the development of novel strategies for treating metabolic disorders and contribute to the advancement of personalized medicine approaches. As the demand for effective therapeutic interventions rises, the characterization of HNF4α and its signaling pathways remains a vital area of research in metabolic health and disease management.
