RXR alpha-LBD (200-462)

• Species: Human
• Expression Host: E. coli
• Tag: His-tag
• Purity: 95%
• Molecular Weight: 32.0 kDa.
• Gene Accession Number: NM_002957.

Purification and Quality Control
The His-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns.
The purified RXR-LBD is greater than 95% homogeneous based on SDS-PAGE analysis.

Unit Definition (Activity)
1 unit equals 1 nanogram purified protein. 20 units are sufficient for an in vitro transcription assay and 100 units are sufficient for a ligand binding or a protein-protein interaction assay.

Applications
RXR-LBD has been applied in in vitro transcription assays, DNA and protein-protein interactions assays.

Formulation and Storage
The protein is in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol. Stored at -70°C before use. Avoid repeated freeze thaw cycles.

Synonym
FLJ00280; FLJ00318; FLJ16020; FLJ16733; MGC102720; NR2B1 and Homo sapiens retinoid X receptor alpha (RXRA).

Protein Sequence
MGMKREAVQE ERQRGKDRNE NEVESTSSAN EDMPVERILE AELAVEPKTE TYVEANMGLN
PSSPNDPVTN ICQAADKQLF TLVEWAKRIP HFSELPLDDQ VILLRAGWNE LLIASFSHRS
IAVKDGILLA TGLHVHRNSA HSAGVGAIFD RVLTELVSKM RDMQMDKTEL GCLRAIVLFN
PDSKGLSNPA EVEALREKVY ASLEAYCKHK YPEQPGRFAK LLLRLPALRS IGLKCLEHLF
FFKLIGDTPI DTFLMEMLEA PHQMT

Background
Retinoid X receptor (RXR) serves as a promiscuous heterodimerization partner for many nuclear receptors through the identity box, a 40-amino acid subregion within the ligand binding domain (LBD). RXR partners include thyroid hormone receptors (TRs), retinoic acid receptors (RARs), peroxisome proliferator-activated receptor, several constitutive active orphan nuclear receptors (e.g. nuclear growth factor I-B), oxysterol receptors, and constitutive androstane receptors. RXRs also form homodimers to mediate the effects of 9-cis-retinoic acid (9-cRA). Depending on these protein-protein interactions, RXR-containing complexes have distinct ligand-dependent and constitutive functions (1, 2). The LBD is functionally complex and mediates ligand binding, receptor homo- and heterodimerization, repression of transcription in the absence of ligand, and ligand-dependent activation of transcription (3). Hormone binding to the structurally conserved LBD of the RXR triggers a conformational change that principally affects the conserved C-terminal transactivation helix H12 involved in transcriptional activation (4). Coactivators directly recruited by liganded receptors include members of the steroid receptor coactivator/p160 family such as SRC-1, transcriptional intermediary factor 2/glucocorticoid receptor interacting protein 1, and RAC3/activator of thyroid and retinoic acid receptors/amplified in breast cancer 1 (5).

Image of SDS-PAGE /Western-blot