Thyroid Hormone receptor,α1 human

NA.26

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: (α) the central, highly conserved, DNA-binding domain (DBD) of approximately 66 amino acids, and (β) 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 TRα and TRβ isoforms, which suggests differential roles in transcriptional regulation. In addition, alternative splicing of the TRβ gene generates two isoforms, TRβ1 and TRβ2 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).

Clear and colorless frozen liquid solution

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

human

expressed in insect cells

≥80% (SDS-PAGE)

frozen liquid

~56.5 kDa

pkg of 5 μg

avoid repeated freeze/thaw cycles

500 μg/mL

clear colorless

NM_003250

P10827

dry ice

−70℃

human ... THRA(7067)

10 - Combustible liquids

WGK 1