Analytical Data
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Gene name
NR1H4
- Application
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Alternative Names
Farnesoid X-activated receptorFarnesol receptor HRR-1Nuclear receptor subfamily 1 group H member 4Retinoid X receptor-interacting protein 14 ;RXR-interacting protein 14
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96RI1
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Expression Region
1-476aa
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Molecular Weight
70.7 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
NR1H4, also known as Liver X Receptor alpha (LXRα), is a nuclear receptor that plays a pivotal role in lipid metabolism, cholesterol homeostasis, and inflammatory responses. It is activated by oxysterols, which are cholesterol derivatives, and functions as a key regulator of genes involved in lipid synthesis, uptake, and efflux. Research into NR1H4 has gained significant attention due to its implications in various metabolic disorders, including dyslipidemia, atherosclerosis, and non-alcoholic fatty liver disease (NAFLD). Understanding the mechanisms by which NR1H4 regulates cholesterol metabolism can aid in the development of therapeutic strategies for these conditions. Moreover, LXRα is also implicated in neuroprotection and the modulation of immune responses, revealing its potential as a target for treatments beyond metabolic diseases. The study of NR1H4 recombinant proteins allows for the elucidation of its structure-function relationships, enabling the exploration of novel ligands and modulators that could enhance its therapeutic potential. Overall, the investigation of NR1H4 recombinant proteins holds promise for advancing our knowledge of metabolic regulation and developing innovative approaches for the treatment of related disorders.
