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Merck

SRP2137

FXR, ligand binding domain (222-472), GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

Sinônimo(s):

FXR, NR1H4, farnesol receptor HRR-1, retinoid receptor

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10 μG

R$ 2.917,00

R$ 2.917,00


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Sobre este item

NACRES:
NA.26
UNSPSC Code:
12352200

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Nome do produto

FXR, ligand binding domain (222-472), GST tagged human, recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

biological source

human

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

form

frozen liquid

mol wt

~56.3 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

400 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)

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Este Item
SRP2128SRP2039SRP2076
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥80% (SDS-PAGE)

assay

≥85% (SDS-PAGE)

biological source

human

biological source

human

biological source

human

biological source

human

concentration

400 μg/mL

concentration

250 μg/mL

concentration

-

concentration

700 μg/mL

mol wt

~56.3 kDa

mol wt

~81.1 kDa

mol wt

~56.6 kDa

mol wt

~35 kDa

form

frozen liquid

form

frozen liquid

form

frozen liquid

form

frozen liquid

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.

Classe de armazenamento

10 - Combustible liquids

wgk

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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