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Key Documents

SRP2019

Sigma-Aldrich

RXR, α human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Synonym(s):

FLJ00280, FLJ16020, FLJ16733, NR2B1

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.26

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

frozen liquid

mol wt

~53 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

400 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... RXRA(6256)

General description

RXRA (retinoid X receptor α) is a member of the nuclear receptor (NR) superfamily, which is the largest known family of transcription factors. All NR family members are defined by two structural components- a central, highly conserved, DNA-binding domain (DBD) composed of ∼66 residues, a C-terminal structurally conserved, ligand-binding domain (LBD) of ∼250 residues. The N-terminal is highly variable and differs from receptor to receptor and contains a ligand-independent transactivation domain known as activation function 1 (AF-1). There are three types of RXR- RXRα, β, and γ.[1][2]

Biochem/physiol Actions

Nuclear receptors form the largest known family of transcription factors and have a crucial role in nearly all aspects of vertebrate development and adult physiology by transducing the effects of hormones into transcriptional responses. The family is defined by two domains: (a) the central, highly conserved, DNA-binding domain (DBD) of approx. 66 amino acids, and (b) the C-terminal, structurally conserved, ligand-binding domain (LBD) of approx. 250 amino acids. In addition to binding to DNA and activating transcription in response to 9-cis retinoic acid, RXR forms heterodimers with the receptors for thyroid hormone (TR), retinoic acid (RAR), vitamin D (VDR), prostanoids (PEAR), and numerous orphan receptors. RXR acts as both activator and repressor of transcription. In the absence of hormone, RXR (homo- or heterodimer) interacts with SMRT (silencing mediator for retinoid and thyroid hormone receptors) and N-CoR (nuclear receptor corepressor) and represses transcription through recruitment of histone deacetylases. In the presence of hormone, RXR interacts with a number of activators including the SRC-1 family, CBP/p300, pCAF and the TRAP complex to target chromatin acetylation and activation of transcription.
RXRA (retinoid X receptor α) functions as a heterodimer partner for multiple nuclear receptors (NR), including constitutive androstane receptor (CAR), the pregnane X receptor (PXR), the peroxisome proliferator-activated receptor-α (PPARα) etc. It also functions as a partner for NRs that are involved in drug and lipid metabolism, and in coordination with MAPK/PI3K (mitogen activated protein kinase/phosphoinositide 3-kinase) is involved in suppression of hepatic detoxification during inflammation.[3] rs10776909 polymorphism in this gene is associated with the pathogenesis of chronic glomerulonephritis (ChGN) and is linked with poorer clinical course of ChGN.[4]

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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Coordinating Role of RXRa in Downregulating Hepatic Detoxification during Inflammation Revealed by Fuzzy-Logic Modeling.
Keller R et al
PLoS Computational Biology, 12(1), e1004431-e1004431 (2016)
Single thyroid hormone receptor monomers are competent for co-activator-mediated transactivation.
Quack M and Carlberg C
The Biochemical Journal, 360(Pt 2), 387-393 (2001)
Association of Retinoid X Receptor Alpha Gene Polymorphism with Clinical Course of Chronic Glomerulonephritis.
Grzegorzewska AE et al
Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 21, 3671-3681 (2015)
General molecular biology and architecture of nuclear receptors.
Pawlak M et al
Current Topics in Medicinal Chemistry, 12(6), 486-504 (2012)
D Moras et al.
Current opinion in cell biology, 10(3), 384-391 (1998-06-26)
In the past few years our understanding of nuclear receptor action has dramatically improved as a result of the elucidation of the crystal structures of the empty (apo) ligand-binding domains of the nuclear receptor and of complexes formed by the

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