SRP2058
FXR-ligand binding domain (222-472) human
recombinant, expressed in E. coli, ≥80% (SDS-PAGE)
Sinónimos:
FXR, Farnesol receptor HRR-1, NR1H4, retinoid receptor
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.26
Productos recomendados
biological source
human
recombinant
expressed in E. coli
assay
≥80% (SDS-PAGE)
form
frozen liquid
mol wt
~31.8 kDa
packaging
pkg of 10 μg
concentration
650 μg/mL
color
colorless to clear
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HRR-1(9971)
Biochem/physiol Actions
Farnesoid-X-activated receptor (FXR) was originally identified and cloned in rat as an orphan nuclear hormone receptor based on hybridization with a degenerate oligonucleotide designed from the highly conserved nuclear hormone receptor DNA binding domain. FXR functions as a heterodimer with RXR and binds to sequence elements in the promoters of target genes. The FXR/RXR heterodimer binds with highest affinity to inverted repeats separated by 1 bp (IR-1) and with low affinity to direct repeats separated by 4 and 5 bp (DR-4 and DR-5). As is the case for other nuclear hormone receptors, FXR regulates target gene activity in response to ligand. While initial studies suggested that farnesol and retinoid metabolites were likely ligands for FXR, current data support the notion that FXR is a bile acid sensor that plays an integral role in bile acid synthesis and transport. In the small intestine, FXR regulates bile acid uptake through the upregulation of the ileal bile acid binding protein gene via binding to an upstream response element. The FXR/RXR heterodimer can be activated by the bile salt chenodeoxycholic acid (CDCA) and FXR is required for the bile salt-dependent transcriptional control of the human ABCB11 gene (the bile salt export pump). In addition, FXR has been shown to inhibit the cholesterol 7-hydrolase gene (CYP7A1) transcription.
Physical form
Clear and colorless frozen liquid solution
Preparation Note
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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W Seol et al.
Molecular endocrinology (Baltimore, Md.), 9(1), 72-85 (1995-01-01)
We have used a yeast genetic system to isolate cDNAs encoding proteins that specifically interact with the ligand-binding domain of human retinoid X receptor-alpha (RXR alpha). A number encoded portions of two known RXR heterodimer partners, the retinoic acid receptor
A M Zavacki et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(15), 7909-7914 (1997-07-22)
Retinoids are crucial regulators of a wide variety of processes in both developing and adult animals. These effects are thought to be mediated by the retinoic acid (RA) receptors and the retinoid X receptors (RXRs). We have identified an additional
B M Forman et al.
Cell, 81(5), 687-693 (1995-06-02)
Nuclear hormone receptors comprise a superfamily of ligand-modulated transcription factors that mediate the transcriptional activities of steroids, retinoids, and thyroid hormones. A growing number of related proteins have been identified that possess the structural features of hormone receptors, but that
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