|Positive WB detected in||Y79 cells, HepG2 cells, mouse eye tissue|
|Positive IHC detected in||human prostate cancer tissue|
Note: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0
|Positive IF detected in||photoreceptor progenitor cells|
|Positive FC detected in||photoreceptor progenitor cells|
|Western Blot (WB)||WB : 1:500-1:2000|
|Immunohistochemistry (IHC)||IHC : 1:20-1:200|
|Immunofluorescence (IF)||IF : 1:20-1:100|
|Sample-dependent, check data in validation data gallery|
14246-1-AP targets NR2E3 in WB, IHC, IF, FC,ELISA applications and shows reactivity with human, mouse, rat, pig samples.
|Tested Reactivity||human, mouse, rat, pig|
|Cited Reactivity||human, mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||NR2E3 fusion protein Ag5503|
|Full Name||nuclear receptor subfamily 2, group E, member 3|
|Calculated molecular weight||45 kDa|
|Observed molecular weight||43-45 kDa|
|GenBank accession number||BC041421|
|Gene ID (NCBI)||10002|
|Purification Method||Antigen affinity purification|
|Storage Buffer||PBS with 0.02% sodium azide and 50% glycerol pH 7.3.|
|Storage Conditions||Store at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage.|
NR2E3, also known as PNR, encodes a retinal nuclear receptor that is a ligand-dependent transcription factor. This protein is part of a large family of nuclear receptor transcription factors involved in signaling pathways. NR2E3 influences the development of photoreceptors and their differentiation into rod and cone types, and acts as a ranscriptional factor that is an activator of rod development and repressor of cone development [PMID:20725840]. It binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. [PMID:15689355]
NR2E3 is a key component in p53 activation by regulating a long noncoding RNA DINO in acute liver injuries.
Loss of NR2E3 represses AHR by LSD1 reprogramming, is associated with poor prognosis in liver cancer.
J Biol Chem
Differential Loss of Prolyl-Isomerase or Chaperone Activity of Ran-binding protein 2 (Ranbp2) Unveils Distinct Physiological Roles of Its Cyclophilin Domain in Proteostasis.
Distinct and Atypical Intrinsic and Extrinsic Cell Death Pathways between Photoreceptor Cell Types upon Specific Ablation of Ranbp2 in Cone Photoreceptors.