"RARG" Related Products

Recombinant Human RARG, Ligand Binding Domain, GST-tagged

Cat. No. : RARG-1138H
Description : Retinoic acid receptors are important in the regulation of growth and differentiation of epithelial tissues, embryonic and central nervous system development and hematopoiesis. Retinoids mediate their effect by two classes of nuclear receptor proteins, the Retinoic Acid Receptors (RARs) and the Retinoid X Receptors (RXRs), that each consist of three isotypes (α,β, and γ) encoded in separate genes. Upon dimerization with RXR, RARs can bind to specific enhancer sequences in the DNA, so-called Retinoic Acid Response Elements (RAREs), resulting in transcriptional activation of target genes in the presence of ligand. The RARγ in the adult is found almost exclusively in the skin. Retinoids affect epidermal cell growth and differentiation as well as sebaceous gland activity and exhibit immunomodulatory and anti-inflammatory properties. Current retinoid research targets the development of receptor-selective retinoids for tailoring and/or improving their therapeutic profile. Recombinant RARγ-LBD was expressed in a baculovirus system and purified by an affinity column in combination with FPLC chromatography.
Source : Sf9 insect cells.
Purity : > 90% by SDS-PAGE.
Form : Liquid. Supplied in 20 mM Tris-HCl pH 8.0, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT and 20% glycerol.
Application : RARγhas been applied in DNA and protein-protein interaction assays.
Storage : Quality guaranteed for 12 months. Store at -80°C.Avoid freeze / thaw cycles.
Usage : For in vitro use only.
Gene Name : RARG retinoic acid receptor, gamma [ Homo sapiens ]
Synonyms : retinoic acid receptor, gamma; RARC; NR1B3; RARG; RAR-gamma; Nuclear receptor subfamily 1 group B member 3
Gene ID : 5916
mRNA Refseq : NM_000966
Protein Refseq : NP_000957
MIM : 180190
UniProt ID : P13631
Chromosome Location : 12q13
Function : metal ion binding; protein binding; retinoic acid receptor activity; retinoid X receptor binding; sequence-specific DNA binding; steroid hormone receptor activity; transcription factor activity; zinc ion binding

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