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SRP2127

Sigma-Aldrich

TR, α1, GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE)

Synonym(s):

AR7, EAR7, ERB-T-1, ERBA, ERBA1, MGC000261, MGC43240, NR1A1, THRA1, c-ERBA-1

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.26

Pricing and availability is not currently available.

biological source

human

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

form

frozen liquid

mol wt

~81.5 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

350 μg/mL

color

clear colorless

NCBI accession no.

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This Item
SRP2046SRP5325SAB4502968
recombinant

expressed in E. coli

recombinant

expressed in insect cells

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

-

assay

≥70% (SDS-PAGE)

assay

≥80% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

-

biological source

human

biological source

human

biological source

human

biological source

rabbit

concentration

350 μg/mL

concentration

500 μg/mL

concentration

-

concentration

~1 mg/mL

mol wt

~81.5 kDa

mol wt

~56.5 kDa

mol wt

~89 kDa

mol wt

antigen 54 kDa

form

frozen liquid

form

frozen liquid

form

buffered aqueous glycerol solution

form

buffered aqueous solution

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 approx. 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 the TR and TR isoforms, which suggests differential roles in transcriptional regulation. In addition, alternative splicing of the TR gene generates two isoforms, TR 1 and TR 2 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. Additionally, 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.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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)

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