Analytical Data
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Gene name
ARNT2
- Application
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Alternative Names
bHLHe1; Class E basic helix-loop-helix protein 1
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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
Q9HBZ2
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Expression Region
Met1~Arg209
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Molecular Weight
30kDa
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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
ARNT2, or Aryl Hydrocarbon Receptor Nuclear Translocator 2, is a member of the bHLH-PAS (basic helix-loop-helix PER-ARNT-SIM) family of transcription factors, playing a crucial role in cellular responses to environmental stimuli and in the regulation of various biological processes, including development, immune response, and metabolism. Research on ARNT2 has gained momentum due to its involvement in various diseases, including cancer and neurological disorders, as well as its potential as a therapeutic target. The reprogramming of ARNT2 into a recombinant protein format enables detailed studies of its structural and functional characteristics, which can provide insights into its mechanisms of action. The expression and purification of ARNT2 as a recombinant protein allow for the evaluation of its interaction with specific ligands, assess its transcriptional regulatory functions, and elucidate its role in mediating responses to xenobiotic agents. Employing advanced techniques like crystallography and NMR spectroscopy can help in visualizing its complex interactions at the molecular level, offering a blueprint for drug development aimed at modulating ARNT2 activity. Moreover, understanding the post-translational modifications and protein-protein interactions of ARNT2 may reveal critical regulatory pathways that could be exploited for therapeutic interventions. Overall, this research presents an exciting avenue for deciphering the multifaceted roles of ARNT2 in health and disease, paving the way for novel strategies to confront associated pathologies.
