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anti-Human CELF2 Antibodies:
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Cow (Bovine) Polyclonal CELF2 Primary Antibody for IHC, WB - ABIN2779001
Subramaniam, Natarajan, Ramalingam, Ramachandran, May, Queimado, Houchen, Anant: Translation inhibition during cell cycle arrest and apoptosis: Mcl-1 is a novel target for RNA binding protein CUGBP2. in American journal of physiology. Gastrointestinal and liver physiology 2008
Overexpression of CELF2 could reverse miR-615-3p's oncogenic functions.
CUG-BP2 binds to AU-rich motifs found in the COX-2 mRNA 3'-UTR.
Study provides evidence for a generalized position- dependent activity of CELF2 in splicing that can be used to predict its consequence on alternative splicing in a cell-type independent manner.
These data suggest an interplay between CELF2 and hnRNP C as the mechanistic basis for activation-dependent alternative splicing of TRAF3 exon 8.
Haplotype-dependent allele-specific methylation of CELF2 gene is associated with neurological disorders.
CUGBP2 expression at the messenger RNA (mRNA) level was 2.2-fold lower and could be associated with high chemoresistance and early dissemination of pancreatic cancer.
the genetic variant rs3740194 in CELF2 gene might be a valuable predictor for NPC prognosis
Data show miR95 expression level positively related to glioma grade and its downregulation affects proliferation, invasion and apoptosis by targeting CELF2. MiR95 is identified as a putative therapeutic target and CELF2 as a potential tumor suppressor.
a widespread role for the JNK-CELF2 axis in controlling splicing during T-cell activation, including a specific role in propagating JNK signaling.
The A allele of rs2242451 in CUGBP2 might decrease Alzheimer disease risk in the Chinese Han population.
novel mechanisms for CELF2 regulation that may broadly impact CELF2 expression across diverse cell types.
There was evidence of association for recently-reported late-onset Alzheimer's disease risk loci, including BIN1 and CLU and CUGBP2 with APOE.
Alternative splicing of LEF1 exon 6 is regulated during pre-TCR signaling in thymic development and in response to activation of the JSL1 T-cell line and this is driven by the activity of CELF2.
results indicate the occurrence of a mis-splicing event in myotonic dystrophy type 1 that is induced neither by a loss of muscleblind-like 1 (MBNL1) function nor by a gain of CUGBP1
BRUNOL3 appears to be an important factor for thymus development and is therefore a candidate gene for the thymus hypoplasia/aplasia seen in partial monosomy 10p patients.
Determination of ETR-3 protein domains required for RNA splicing.
data suggest that CUGBP2 is a critical regulator of the apoptotic response to genotoxic injury in breast cancer cells
Lipopolysaccharide inhibition of CUGBP2 is a prostaglandin-dependent mechanism.
Developmental upregulation of apoB mRNA editing from approximately 3% to 88% begins with decreased levels of inhibitory CUG binding protein 2 (CUGBP2) expression.
CUGBP2 overrides HuR and suppresses COX-2 mRNA translation.
CELF1 and CELF2 may underlie conserved, developmentally regulated, tissue-specific processes in vertebrate embryos
Napor-3 suppression by ethanol during mid and late stage fetal brain converts natural physiological event apoptosis into a pathological process.
Colonic MSCs expressed high Ptgs2 levels as a consequence of mRNA stabilization downstream of Fgf9. This stabilization was mediated partially through a mechanism involving endogenous CUG-binding protein 2.
A renmarkable decrease in CUG-binding protein-2 (Cugbp2) expression is seen in the pyramidal cells of the hippocampus following neuronal degeneration.
NAPOR may be one of a group of closely related proteins involved in splicing regulation within the brain.
Data demonstrate that cells expressing CUGBP2 variant 1 undergo apoptosis during mitosis, suggesting mitotic catastrophe.
CUGBP2 interacts with functionally significant RNA motifs surrounding the branch sites upstream of exon 6 of the CUGBP2 transcript itself.
Cloning and expression of Napor/CUG-BP2 in embryo development.
Members of the CELF/BRUNOL protein family contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation. Alternative splicing results in multiple transcript variants encoding different isoforms.
CUG triplet repeat, RNA binding protein 2
, CUG triplet repeat RNA-binding protein 2
, CUG-BP- and ETR-3-like factor 2
, CUGBP Elav-like family member 2
, ELAV-type RNA-binding protein 3
, RNA-binding protein BRUNOL-3
, bruno-like protein 3
, neuroblastoma apoptosis-related RNA-binding protein
, elav-type RNA-binding protein 3
, CUG triplet repeat, RNA binding protein 2-a
, Cugbp- and Etr3-like factor 2
, RNA-binding protein Brunol3
, CUG triplet repeat RNA binding protein 2