SRP2020
TR, β 1 isoform human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE)
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Synonym(s):
ERBA-beta, GRTH, NR1A2, THR1, THRB1
UNSPSC Code:
12352202
NACRES:
NA.26
biological source
human
recombinant
expressed in E. coli
assay
≥70% (SDS-PAGE)
form
frozen liquid
mol wt
~53 kDa
packaging
pkg of 10 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
500 μg/mL
color
clear colorless
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... THRB(7068)
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 approximately 66 amino acids, and (b) the C-terminal, structurally conserved, ligand-binding domain (LBD) of approximately 250 amino acids. The amino-terminal regions are least conserved among nuclear receptor sequences. This domain is highly divergent between TR α and TR β isoforms, which suggests differential roles in transcriptional regulation. In addition, alternative splicing of the TR β gene generates two isoforms, TR β1 and TR β2 with completely different amino-terminal domains. Unliganded TR inhibits the formation of a functional pre-initiation complex, through direct interaction with TBP and transcription factor IIB. In addition, in the absence of ligand TR has been shown to repress transcription through recruitment of a corepressor complex, which also includes Sin3A and histone deacetylase. Ligand binding releases the corepressor complex and recruits a coactivator complex that includes multiple histone acetyltransferases, including a steroid receptor family coactivator, p300/CREB-binding protein–associated factor (PCAF), and CREB binding protein (CBP).
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.
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers.
C K Glass
Endocrine reviews, 15(3), 391-407 (1994-06-01)
The nuclear receptor superfamily: the second decade.
D J Mangelsdorf et al.
Cell, 83(6), 835-839 (1995-12-15)
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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