Retinoic Acid Receptor Beta (RARβ; NR1B2)
INDIGO’s Human Retinoic Acid Receptor Beta (RARβ) Reporter Assay System utilizes proprietary mammalian cells engineered to provide constitutive, high-level expression of human RARβ (NR1B2), a ligand-dependent transcription factor. Because these cells incorporate a responsive luciferase reporter gene, quantifying expressed luciferase activity provides a sensitive surrogate measure of RARβ activity in treated cells. The primary application of this reporter assay system is in the screening of test samples to quantify functional activity, either agonist or antagonist, that they may exert against human RARβ.
Retinoic acid receptors (RARs) are nuclear hormone receptors of the NRB1 class, which function as heterodimers with retinoid X receptors (RXRs). There are three distinct RAR subtypes; RARalpha, RARbeta and RARgamma. RARalpha is present in most tissue types, whereas RARbeta and RARgamma expression is more selective. RXR-RAR heterodimers act as ligand-dependent transcriptional regulators by binding to the specific retinoic acid response element (RARE) found in the promoter regions of target genes. In the absence of an RAR agonist, RXR-RAR recruits co-repressor proteins such as NCoR and associated factors such as histone deacetylase to maintain a condensed chromatin structure. RAR agonist binding stimulates co-repressor release and co-activator complexes, such as histone acetyltransferase, are recruited to activate transcription. RARs transduce retinoid signals in vivo, which mediates proper embryogenesis, differentiation and growth arrest. Specifically, RXRalpha-RARgamma heterodimers are necessary for growth arrest and viseral and primitive endodermal differentiation, whereas RXRalpha-RARalpha is required for cAMP-dependent parietal endodermal differentiation. In vitro it has been difficult to elucidate the roles of individual subtypes as functional RAR knockouts generate artificial redundancies that are thought not to exist under normal conditions.
For more information on RARβ, visit the Nuclear Receptor Resource.
Kits are offered in different assay formats to accommodate researchers’ needs: 3x 32, 1x 96, and 1x 384 assay formats for screening small numbers of test compounds, as well as custom bulk reagents for HTS applications. Assay systems are all inclusive, providing reporter cells, optimized growth media, media for diluting test compounds, a positive-control agonist, luciferase detection reagent, a white assay plate, a detailed protocol, and a protocol quick guide. All kits are shipped on dry ice.
RARβ Reporter Cells are prepared using INDIGO’s proprietary CryoMite™ process. This cryo-preservation method yields high cell viability post-thaw, and provides the convenience of immediately dispensing healthy, division-competent reporter cells into assay plates. There is no need for intermediate spin-and-wash steps, viability determinations, or cell titer adjustments.
This kit product is an all-inclusive assay system that includes, in addition to RARβ Reporter Cells, two optimized media for use during cell culture and (optionally) in diluting the test samples, a reference agonist, Luciferase Detection Reagent, a cell culture-ready assay plate, and a detailed protocol.
|Product Family||Product Number||Product Description|
|IB0210 RARβ (NR1B2)||IB02101-32||Human RARβ Reporter Assay System, 3 x 32 assays in 96-well format|
|IB02101||Human RARβ Reporter Assay System, 1 x 96-well format assays|
|IB02102||Human RARβ Reporter Assay System, 1 x 384-well format assays|
Service Assays: Human
The primary application of INDIGO’s cell-based nuclear receptor assays are to quantitatively assess the bioactivity of a test compound as an agonist (activator) or antagonist (inhibition of an agonist response) of a given receptor. Service assays include a positive control reference compound and ‘vehicle’ control for every experiment. A formal study report and all data files are provided to the client upon completion of the study. To receive a quote for your proposed study, complete & submit the online “Request a Quote” form or contact an INDIGO Customer Service Representative to discuss your desired study parameters. To initiate a Service Study, download and complete all fields of the Excel worksheet “Service Work Order" then submit the electronic file to INDIGO Customer Service.
Development and characterization of novel and selective inhibitors of cytochrome P450 CYP26A1, the human liver retinoic acid hydroxylase
ABSTRACT Cytochrome P450 CYP26 enzymes are responsible for all-trans-retinoic acid (atRA) clearance. Inhibition of CYP26 enzymes will increase endogenous atRA concentrations and is an attractive therapeutic target. However, the selectivity and potency of the existing atRA metabolism inhibitors towards CYP26A1 and CYP26B1 is unknown, and no selective CYP26A1 or CYP26B1 inhibitors have been developed. Here
Triphenyl phosphate-induced developmental toxicity in zebrafish: Potential role of the retinoic acid receptor
ABSTRACT Using zebrafish as a model, we previously reported that developmental exposure to triphenyl phosphate (TPP) – a high-production volume organophosphate-based flame retardant – results in dioxin-like cardiac looping impairments that are independent of the aryl hydrocarbon receptor. Using a pharmacologic approach, the objective of this study was to investigate the potential role of retinoic
View Full Size Research conducted by: Prajakta Albrecht (1), Koji Toyokawa (1), Ewa Maddox (1), Palmer Cramer (1), Jack Vanden Huevel (1,2), & Bruce Sherf (1) (1) INDIGO Biosciences, Inc., 1981 Pine Hall Rd, State College, PA, USA (2) Center for Molecular Toxicology and Carcinogenesis, 325 Life Sciences Building, Penn State University, University Park, PA 16802,
ABSTRACT Vitamin A (retinol) and its metabolites play many physiological roles including cell differentiation, cell proliferation, energy homeostasis, circadian rhythm and immune response. Vitamin A and its metabolites are known to act through retinoid acid receptors (RARs), retinoid-related orphan receptors (RORs) and retinoid x receptors (RXRs). These receptors are also important drug targets, although the