Analytical Data
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Gene name
FXR
- Application
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Alternative Names
NR1H4; BAR; FXR; HRR1; RIP14; Nuclear Receptor Subfamily 1,Group H,Member 4; Bile acid receptor; Farnesol receptor HRR-1; Retinoid X receptor-interacting protein 14
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Species
Mouse
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q60641
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Expression Region
Leu212~Gln488
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Molecular Weight
53kDa
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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
Farnesoid X receptor (FXR), a member of the nuclear receptor superfamily, plays a critical role in regulating bile acid metabolism, lipid homeostasis, and glucose metabolism, positioning it as a promising target for therapeutic interventions in metabolic diseases. FXR is primarily expressed in the liver and intestines, where it governs the transcription of genes involved in bile acid synthesis and transport, thus maintaining bile acid homeostasis. The importance of FXR in disease contexts, such as non-alcoholic fatty liver disease (NAFLD) and cholestasis, has sparked increased interest in its regulatory mechanisms. Recent research has focused on the design and synthesis of FXR recombinant proteins to elucidate its structural and functional properties. These recombinant FXR proteins are employed in various assays to study ligand binding, gene transcriptional regulation, and protein-protein interactions, providing valuable insights into the receptor's physiological roles. Additionally, the development of FXR agonists is being explored as a potential therapeutic strategy to combat metabolic disorders, highlighting the necessity for a deeper understanding of FXR’s mechanisms via recombinant technology. Overall, studying FXR recombinant proteins facilitates advancements in the search for novel interventions against metabolic and liver-related diseases.
