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Key Documents

SRP2159

Sigma-Aldrich

Rev-ErbA, β (RVR) human

recombinant, expressed in insect cells, ≥80% (SDS-PAGE)

Synonim(y):

BD73, EAR-1R, RVR

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About This Item

Kod UNSPSC:
12352202
NACRES:
NA.26

pochodzenie biologiczne

human

rekombinowane

expressed in insect cells

Próba

≥80% (SDS-PAGE)

Postać

frozen liquid

masa cząsteczkowa

~66.6 kDa

opakowanie

pkg of 5 μg

warunki przechowywania

avoid repeated freeze/thaw cycles

stężenie

350 μg/mL

kolor

clear colorless

numer dostępu NCBI

numer dostępu UniProt

Warunki transportu

dry ice

temp. przechowywania

−70°C

informacje o genach

human ... NR1D2(9975)

Działania biochem./fizjol.

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. Members of the steroid/thyroid hormone nuclear receptor (NR) superfamily bind specific DNA elements and function as ligand activated transcription factors. This group includes the `orphan receptors′ which have no known ligands in the `classical sense′ and appear to be the ancient progenitors of this receptor superfamily. The Rev-erb family of proteins are orphan members of the receptor superfamily. Two isoforms of the Rev-erb family have been isolated from mammalian genotypes, Rev-erbA[alpha] and Rev-erbA[beta]/RVR. Major differences between the two isoforms occur within the hyper-variable A/B and D regions of the proteins. Both isoforms are expressed in a wide range of tissues and are present in all major organs. Rev-erbA[alpha] mRNA is upregulated during adipocyte differentiation but repressed during myogenesis. These orphan receptors are closely related to the ROR/RZR[alpha] gene family (retinoic acid receptor related orphan receptor) and the Drosophila orphan receptor, E75A, particularly in the DNA-binding domain (DBD) and the putative ligand-binding domain (LBD). RVR and Rev-erbA[alpha] bind as monomers to an asymmetric ( A / T ) 6 RGGTCA motif. The Rev-erb family has also been demonstrated to bind as homodimers to novel HREs consisting of two tandemly arranged AGGTCA motifs, separated by 2 bp with unique 5′ flanking and spacer nucleotides (RevDR-2). Reports on the transcriptional properties of the Rev-erb family were initially conflicting. Rev-erbA[alpha] was first reported to act as a constitutive activator of transcription through its cognate monomeric asymmetric motif. Recently, it has been demonstrated that members of the Rev-erb family are, in fact, dominant repressors of transcription. Rev-erbA[beta] is expressed in the central nervous system, skeletal and dorsal muscles, spleen and mandibular and maxillar processes. During embryogenesis RVR is expressed in the notochord and neural tube, but its function/role during differentiation and mammalian development remains obscure.

Postać fizyczna

Clear and colorless frozen liquid solution

Uwaga dotycząca przygotowania

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

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

R M Evans
Science (New York, N.Y.), 240(4854), 889-895 (1988-05-13)
Analyses of steroid receptors are important for understanding molecular details of transcriptional control, as well as providing insight as to how an individual transacting factor contributes to cell identity and function. These studies have led to the identification of a
M A Lazar et al.
Molecular and cellular biology, 9(3), 1128-1136 (1989-03-01)
A cDNA encoding a novel member of the thyroid/steroid hormone receptor superfamily, called Rev-ErbA alpha, has been isolated from a rat GH3 cell library. Rev-ErbA alpha is an approximately 56-kilodalton protein most similar in structure to the thyroid hormone receptor
The nuclear receptor superfamily: the second decade.
D J Mangelsdorf et al.
Cell, 83(6), 835-839 (1995-12-15)

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