Thyroid hormone nuclear receptors (TRs) are ligand-dependent transcription factors which regulate and control many metabolic and developmental processes. There are two genes encoding TRs identified to date, TRα and TRβ. TRs bind to thyroid hormone response elements (TREs) with half-site binding motifs in the orientation of palindromes, direct repeats or inverted palindromes. The affinities of binding are both variable and influenced differentially by 3,5,3''-triiodo-L-thyronine (T3). Transcriptional regulation by TRs is also modulated by heterodimerization with TR nuclear accessory proteins, the most extensively characterized of which are the retinoid X receptors (RXRα, RXRβ and RXRγ). The TRα isoform TRα1 can display both a nuclear and undefined cytoplasmic location, and is the only TR that is imported into the mitochondrial matrix. TRα2 is a C-terminal variant of TRα1 that does not bind thyroid hormones (THs) and weakly binds DNA. TRα2 acts as a dominant negative antagonist of TH signalling.

Thyroid hormone receptor alpha; Nuclear receptor subfamily 1 group A member 1; V-erbA-related protein 7; EAR-7; c-erbA-1; c-erbA-alpha

p10827

Human,Pig

WB,IF,ICC

WB 1:2000-1:5000
IF 1:50-1:200
ICC 1:100-1:400

~ 58 kDa

Rabbit

This antibody detects endogenous levels of TRα protein.

Synthetic peptide, corresponding to Human TRα.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.