SRP2049
RAR, γ human
recombinant, expressed in insect cells, ≥80% (SDS-PAGE)
Sinonimo/i:
NR1B3, RARC
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About This Item
Codice UNSPSC:
12352202
NACRES:
NA.26
Origine biologica
human
Ricombinante
expressed in insect cells
Saggio
≥80% (SDS-PAGE)
Forma fisica
frozen liquid
PM
~52.1 kDa
Confezionamento
pkg of 5 μg
Condizioni di stoccaggio
avoid repeated freeze/thaw cycles
Concentrazione
250 μg/mL
Colore
clear colorless
N° accesso NCBI
N° accesso UniProt
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
Informazioni sul gene
bovine ... RARG(5916)
Azioni biochim/fisiol
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.
Stato fisico
Clear and colorless frozen liquid solution
Nota sulla preparazione
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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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