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Merck

SRP2049

Sigma-Aldrich

RAR, γ human

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

Synonym(e):

NR1B3, RARC

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About This Item

UNSPSC-Code:
12352202
NACRES:
NA.26

Biologische Quelle

human

Rekombinant

expressed in insect cells

Assay

≥80% (SDS-PAGE)

Form

frozen liquid

Mol-Gew.

~52.1 kDa

Verpackung

pkg of 5 μg

Lagerbedingungen

avoid repeated freeze/thaw cycles

Konzentration

250 μg/mL

Farbe

clear colorless

NCBI-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−70°C

Angaben zum Gen

bovine ... RARG(5916)

Biochem./physiol. Wirkung

Retinoic acid receptors are important in the regulation of growth and differentiation of epithelial tissues, embryonic and central nervous system development and hematopoiesis. Retinoids mediate their effect by two classes of nuclear receptor proteins, the retinoic acid receptors (RARs) and the retinoid X receptors (RXRs), that each consist of three isotypes (α, β, and γ) encoded in separate genes. Upon dimerization with RXR, RARs can bind to specific enhancer sequences in the DNA, so-called retinoic acid response elements (RAREs), resulting in transcriptional activation of target genes in the presence of ligand. The RAR-gamma in the adult is found almost exclusively in the skin. Retinoids affect epidermal cell growth and differentiation as well as sebaceous gland activity and exhibit immunomodulatory and anti-inflammatory properties. Current retinoid research targets the development of receptor-selective retinoids for tailoring and/or improving their therapeutic profile.

Physikalische Form

Clear and colorless frozen liquid solution

Angaben zur Herstellung

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

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (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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