Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human MBNL1 Protein expressed in HEK-293 Cells - ABIN2725584
Echeverria, Cooper: Muscleblind-like 1 activates insulin receptor exon 11 inclusion by enhancing U2AF65 binding and splicing of the upstream intron. in Nucleic acids research 2014
Mbnl1(+/-); Mbnl2 (show MBNL2 Proteins)(+/-) knockout mice with myotonic dystrophy presented with clinical myofibril ultrastructural abnormality and cardiac arrhythmias.
our study uncovered a novel, autoregulatory function of MBNL proteins based on their binding to e1 of MBNL1 transcript. This function might facilitate cellular protection from MBNL protein level fluctuations, which might otherwise lead to adverse effects caused by extreme MBNL content.
Data show that Muscleblind-like 1 (Mbnl1) and Muscleblind-Like 3 (Mbnl3 (show MBNL3 Proteins)) bind skeletal muscle chloride channel (show CLCA1 Proteins) CIC-1 (Clc-1 (show CLCN1 Proteins)) mRNA.
Depletion of Mbnl1 and/or Mbnl2 (show MBNL2 Proteins) reduced localization of hundreds of transcripts, implicating Mbnls in localization of mRNAs to neurites
Sense DMPK (show DMPK Proteins) RNA foci clearly co-localize with MBNL1 and MBNL2 (show MBNL2 Proteins) proteins and accumulate in myotonic dystrophy 1 tissues during development.
MBNL1 overexpression promotes transformation of fibroblasts into myofibroblasts.
These data indicate that MBNL1 plays a conserved role in negatively regulating TGFbeta (show TGFB1 Proteins) signaling, and is required for normal valve morphogenesis and homeostasis in vivo.
this study supports a key role for Mbnl1 loss in the initiation of DM1 cardiac disease.
Differential expression of Mbnl1 in development plays a role in alternative splicing of vesicular trafficking genes in postnatal heart development.
Results show that nuclear localization is a major determinant of MBNL1 function. It promotes the nuclear retention of repeat-containing transcripts, which results in repression of aberrant protein expression from the expanded repeats.
RAN Translation Regulated by Muscleblind Proteins in Myotonic Dystrophy Type 2
Our work suggests that DM1 (show DMPK Proteins) patients are at risk for Fuchs' endothelial corneal dystrophy (FECD (show COL8a2 Proteins)). DMPK (show DMPK Proteins) mutations contribute to the genetic burden of FECD (show COL8a2 Proteins) but are uncommon. We establish a connection between two repeat expansion disorders converging upon RNA-MBNL1 foci and FECD (show COL8a2 Proteins).
Binding of the MBNL zinc fingers to cardiac troponin T (show TNNT2 Proteins) pre-mRNA is specific and relatively simple, unlike the complex multiple dimer-trimer stoichiometries postulated in some previous studies.
Heterozygous missense mutations and one in-frame deletion in MBNL1 were identified in 3 myotonic dystrophy patients.
Nuclear retention of full-length HTT (show HTT Proteins) RNA is mediated by splicing factors MBNL1 and U2AF65 (show U2AF59 Proteins)
muscleblind-like 1 (MBNL1) is a robust suppressor of multiorgan breast cancer metastasis. It binds the 3' untranslated regions of DBNL (show DBNL Proteins) and TACC1 (show TACC1 Proteins) -two genes that are implicated as metastasis suppressors.
abnormal splicing of DMD (show DMD Proteins) exon 78 found in dystrophic muscles of DM1 (show DMPK Proteins) patients is due to the functional loss of MBNL1 and leads to the re-expression of an embryonic dystrophin (show DMD Proteins) in place of the adult isoform.
Reduced RBFOX1 (show A2BP1 Proteins) activity in myotonic dystrophy type 1 tissues may amplify several of the splicing alterations caused by the deficiency in MBNL1.
MBNL1 binds with C allelic pre-miR (show MLXIP Proteins)-1307 leading to low expression of miR (show MLXIP Proteins)-1307-3p in colorectal cancer.
Involved in pre-mRNA alternative splicing regulation. Binds to CUG triplet repeat in RNA (By similarity).
, muscleblind-like (Drosophila)
, muscleblind-like protein 1
, muscleblind-like 1
, triplet-expansion RNA-binding protein