Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human CELF1 Antibodies:
anti-Mouse (Murine) CELF1 Antibodies:
anti-Rat (Rattus) CELF1 Antibodies:
Go to our pre-filtered search.
Cow (Bovine) Monoclonal CELF1 Primary Antibody for FACS, GS - ABIN152357
Kress, Gautier-Courteille, Osborne, Babinet, Paillard: Inactivation of CUG-BP1/CELF1 causes growth, viability, and spermatogenesis defects in mice. in Molecular and cellular biology 2007
Show all 11 Pubmed References
Human Polyclonal CELF1 Primary Antibody for IHC - ABIN965946
Timchenko, Miller, Timchenko, DeVore, Datar, Lin, Roberts, Caskey, Swanson: Identification of a (CUG)n triplet repeat RNA-binding protein and its expression in myotonic dystrophy. in Nucleic acids research 1997
Show all 7 Pubmed References
Human Polyclonal CELF1 Primary Antibody for IHC - ABIN965947
Good, Chen, Warner, Herring: A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator. in The Journal of biological chemistry 2000
Show all 7 Pubmed References
results underscore novel roles of CELF1 in melanoma, illustrating tumor type-restricted functions of mRNA binding proteins in cancer.
These data present an 11-component genetic pathway, invisible to transcriptional profiling approaches, in which the CELF1 protein functions as a central node controlling translational activation of genes driving EMT and ultimately tumour progression.
High CELF1 expression is associated with aberrant splicing in Type 1 diabetes.
CELF1 globally regulates the alternative splicing.
Findings indicate that IGF2R expression is controlled posttranscriptionally by two factors that associate with Igf2r mRNA and suggest that miR-195 and CUGBP1 dampen IGF signaling by inhibiting IGF2R translation.
In the course of these studies, we found that RNA binding protein CUGBP1 is a new tumor suppressor protein which is reduced in all HBL samples. Therefore, we generated CUGBP1 KO mice and examined HBL signatures in the liver of these mice. Micro-array studies revealed that the HBL-specific molecular signature is developed in livers of CUGBP1 KO mice at very early ages
Results show that CELF1 is a potential target of TUG1 interaction and could be negatively regulated by TUG1 RNA.
CUG-binding protein 1 regulates HSC activation and liver fibrogenesis.
High expression of CUGBP1 is associated with recurrence in lung adenocarcinoma.
CUG-BP1 affected the calcium release activity in single myofibers and the extent of atrophy was significantly reduced upon gene silencing of CUG-BP1 in atrophic muscle.
these data provided a comprehensive view of the CELF1 mRNA regulatory network in oral cancer
forced expression of miR-214-3p enhances the sensitivity of esophageal cancer cells to cisplatin-induced apoptosis. This effect is abrogated with rescue expression of survivin or CUG-BP1
Expression of several genes within the CELF1 locus, including MTCH2, were highly correlated with one another and were associated with Alzheimer's disease status.
CUGBP1 and HuR negate each other's effects in regulating E-cadherin translation by altering the recruitment of E-cadherin mRNA to PBs and play important roles in the regulation of intestinal barrier integrity.
CUGBP1 promotes cell proliferation and suppresses apoptosis via down-regulating C-EBPalpha in human non-small cell lung cancers.
The results indicate that the cellular level of miR-122 is determined by the balance between the opposing effects of GLD-2 and PARN/CUGBP1 on the metabolism of its 3'-terminus.
CELF1 dysfunction in malignant T cells led to the up-regulation of a subset of GRE-containing transcripts that promote cell growth and down-regulation of another subset that suppress cell growth
Celf1 has a role in vegetal RNA localization during Xenopus oogenesis
These results demonstrate the importance of CUGBP1 in the biological and pathological functions of NSCLC and indicate its potential as a therapeutic target for NSCLC.
The result is consistent with the hypothesis that MBNL proteins are trapped by expanded CUG repeats and inactivated in myotonic dystrophy type 1 (DM1) and that CELF1 is activated in DM1.
These results indicate that CELF1 target RNAs are aberrantly spliced in the Type 1 diabetic heart leading to abnormal gene expression.
this study shows that the absence of Celf1 causes neonatal cardiac dysfunction and transcriptome changes
Results found that the blood level of CUGBP1 in mice was decreased during the progression of acute myocardial infarction (AMI) and demonstrate that CUGBP1 is functionally important in AMI. This finding reveals the roles of CUGBP1 in the heart not only during development but also in cardiac disease.
Increased CELF1 expression down-regulates Cx43 mRNA level in the dilated cardiomyopathy heart.
lncBATE10 can decoy Celf1 from Pgc1alpha, thereby protecting Pgc1alpha mRNA from repression by Celf1
Study concludes that CUGBP1 is a critical regulator of insulin secretion via activating PDE3B.
the oncoprotein gankyrin (Gank) preferentially binds to and triggers degradation of dephosphorylated CUGBP1 (de-ph-S302-CUGBP1) or S302A mutant CUGBP1.
Our studies support the existence of an RNA regulon containing Signal Recognition Particle mRNAs that is controlled by CELF1. One implication is that altered function of CELF1 in myotonic dystrophy may contribute to changes in the extracellular matrix of affected muscle through defects in secretion
CELF1 downregulates Cyp19a1 (Aromatase) posttranscriptionally to achieve high concentrations of testosterone compatible with spermiogenesis completion.
developmental stage-specific compatibility of CELF-dependent splice variants dictates their effects on cardiac health and function
Differential expression of CELF1 in development plays a role in alternative splicing of vesicular trafficking genes in postnatal heart development.
Celf1 plays a distinctive and negative role in terminal myocyte differentiation, which partially contribute to DM1 RNA toxicity.
These results indicate that JNK2 is essential for maintenance of normal intestinal epithelial homeostasis and maturation under biological conditions by differentially modulating HuR and CUGBP1.
CELF1 and CELF2 may underlie conserved, developmentally regulated, tissue-specific processes in vertebrate embryos
Mitochondrial biogenesis occurs in the presence of increased CUG-BP1 and AUF1, suggesting that reductions in known mRNA destabilizing proteins likely does not contribute to exercise-induced mitochondrial biogenesis.
these results strongly support a role for -mediated alternative splicing in the regulation of contractile gene expression, achieved in part through modulating the activity of SRF, a key cardiac transcription factor.
This review is focused on the role of a conserved, multifunctional RNA-binding protein, CUGBP1, in the development of aging phenotype in the liver.
disruption of Celf1 gene is also responsible for a fully penetrant delayed first wave of spermatogenesis, and a delay of steroidogenesis may be the cause for the delay of germ cells differentiation
Dysregulation of CELF-mediated alternative splicing programs may be responsible for the disruption of these properties during muscle pathogenesis.
CUGBP1 associates with GU-rich elements to regulate decay of a wide range of mRNAs.
Results therefore suggest that Celf1 regulates proper organogenesis of endoderm-derived tissues by regulating the expression of such targets.
Celf1-dependent fine-tuning of dmrt2a expression is essential for generating bilateral symmetry of somites and left-right asymmetric patterning during zebrafish development.
not only mRNA but also protein of brul is localized to the zebrafish germ plasm at the ends of the cleavage furrows
This "target protector and rescue assay" demonstrates that the phenotypic defects associated with CUGBP1 inactivation in Xenopus are essentially due to the deregulation of Su(H) mRNA.
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. This gene may play a role in myotonic dystrophy type 1 (DM1) via interactions with the dystrophia myotonica-protein kinase (DMPK) gene. Alternative splicing results in multiple transcript variants encoding different isoforms.
CUG triplet repeat, RNA binding protein 1
, CUGBP Elav-like family member 1
, 50 kDa nuclear polyadenylated RNA-binding protein
, CUG RNA-binding protein
, CUG triplet repeat RNA-binding protein 1
, CUG triplet repeat, RNA-binding protein 1
, CUG-BP- and ETR-3-like factor 1
, EDEN-BP homolog
, RNA-binding protein BRUNOL-2
, bruno-like 2
, bruno-like protein 2
, deadenylation factor CUG-BP
, embryo deadenylation element binding protein
, embryo deadenylation element-binding protein homolog
, nuclear polyadenylated RNA-binding protein, 50-kD
, brain protein F41
, deadenylation factor EDEN-BP
, EDEN-BP/Bruno-like protein
, CUG triplet repeat RNA-binding protein 1-A
, CUG-BP- and ETR-3-like factor 1-A
, CUGBP Elav-like family member 1-A
, RNA-binding protein BRUNOL-2-A
, bruno-like protein 2-A
, embryo deadenylation element-binding protein A