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SRP2049

Sigma-Aldrich

RAR, γ human

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

Sinónimos:

NR1B3, RARC

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

biological source

human

recombinant

expressed in insect cells

assay

≥80% (SDS-PAGE)

form

frozen liquid

mol wt

~52.1 kDa

packaging

pkg of 5 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

250 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

Storage temp.

−70°C

Gene Information

bovine ... RARG(5916)

Biochem/physiol Actions

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.

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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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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