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About This Item
NACRES:
NA.26
UNSPSC Code:
12352200
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.
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. rs10776909 polymorphism in this gene is associated with the pathogenesis of chronic glomerulonephritis (ChGN) and is linked with poorer clinical course of ChGN.
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
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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)
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)
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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