产品名称
RAR, γ human, recombinant, expressed in insect cells, ≥80% (SDS-PAGE)
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.
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers.
C K Glass
Endocrine reviews, 15(3), 391-407 (1994-06-01)
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
The nuclear receptor superfamily: the second decade.
D J Mangelsdorf et al.
Cell, 83(6), 835-839 (1995-12-15)
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