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anti-Human PTBP1 Antikörper:
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Human Polyclonal PTBP1 Primary Antibody für WB - ABIN1881702
Osada, Uno, Mineta, Kameoka, Takahashi, Terao: Ancient genome-wide admixture extends beyond the current hybrid zone between Macaca fascicularis and M. mulatta. in Molecular ecology 2010
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Human Polyclonal PTBP1 Primary Antibody für IHC (p), IHC - ABIN250017
Cote, Zhu, Thomas, Martin, Murad, Sharina: Hydrogen peroxide alters splicing of soluble guanylyl cyclase and selectively modulates expression of splicing regulators in human cancer cells. in PLoS ONE 2012
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Cow (Bovine) Polyclonal PTBP1 Primary Antibody für WB - ABIN2778815
Somberg, Zhao, Fröhlich, Evander, Schwartz: Polypyrimidine tract binding protein induces human papillomavirus type 16 late gene expression by interfering with splicing inhibitory elements at the major late 5' splice site, SD3632. in Journal of virology 2008
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Dog (Canine) Polyclonal PTBP1 Primary Antibody für ELISA, WB - ABIN547147
Charlet-B, Logan, Singh, Cooper: Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing. in Molecular cell 2002
experimental analysis of specimens from 3 different brain tumor groups and 1 reactive gliosis group indicates the feasibility of using anti-PTBP1 antibody in diagnostic neuropathology, and computerized image analysis provides a systematic and quantitative approach to explore feasibility
study provides evidence for the role of PTB in keloid pathophysiology and offers a novel therapeutic target for keloids. Most importantly, the role TGF-beta1 regulation of PTB may provide new insights into the mechanisms underlying inflammatory cytokine-induced fibrosis.
the study revealed that PTBP1 facilitates colorectal cancer migration and invasion activities by inclusion of cortactin exon 11
Results showed the expression level of PTBP1 were increased in bladder cancer (BC) patients and that its expression is negatively regulated by MIR-145.
PTBP1 is a novel regulator of MCL1 mRNA by which it controls apoptotic response to antitubulin chemotherapeutics.
PTB interacts specifically with 3'UTR of p53 mRNA and positively regulates expression of p53 isoforms. PTB showed some overlapping binding regions in the p53 3'UTR with miR-1285. Knockdown of miR-1285 as well as expression of p53 3'UTR with mutated miR-1285 binding sites resulted in enhanced association of PTB with the 3'UTR, which provides mechanistic insights of this interplay.
It has been established that PTBP1 and PTBP2 are members of a family of cryptic exon repressors.
These results demonstrate that during early stages of splicing, exon RNP complexes are highly dynamic with many proteins failing to bind during PTBP1 arrest.
Studied interactions of polypyrimidine tract-binding protein (PTBP1), pyruvate kinase M2 (PKM2), and STAT3 (signal transducer and activator of transcription 3) in oncogenesis of anaplastic large cell lymphoma (ALCL). Results show that in ALCL cells, PTBP1 is crucial for PKM2 phosphorylation of STAT3 in the nucleus.
Expression of ATG10 negatively regulated by PTBP1 and is associated with metastasis of colorectal cancer cells.
Polypyrimidine tract binding protein (PTBP1) is a heterogeneous nuclear ribonucleoprotein (hnRNP) that plays roles in most stages of the life-cycle of pre-mRNA and mRNAs in the nucleus and cytoplasm.
follow-up molecular analyses of one splicing factor PTBP1 revealed its impact on disease-associated splicing patterns in Huntington's disease (HD). Collectively, our data provide genomic evidence for widespread splicing dysregulation in HD brains, and suggest the role of aberrant alternative splicing in the pathogenesis of HD
CD5 transcription is increased, leading to the production of three mRNA isoforms by APA, all contributing for protein production, at different levels. PTBP1 binds in the vicinity of pA1, leading to an increase in mRNA levels and miR-204 targets the longer CD5 mRNA.
Increased expression of microRNA miR-145 combined with knockdown of PTBP1 protein contributed to the greater and longer growth suppression compared with each single treatment.
MiR-133b switched the PKM isoform expression from PKM2 to PKM1 through the silencing of PTBP1, which is an alternative splicer of PKM, leading to growth suppression through the induction of autophagy in part by the metabolic switching from glycolysis to oxidative phosphorylation for a short period of time.
Results suggested that PTBP1 and PTBP1-associated miR-1 and -133b are crucial molecules for the maintenance of the Warburg effect in colorectal tumors.
The polypyrimidine tract binding protein 1 (PTBP1) shields specific retroviral and cellular transcripts from nonsense-mediated mRNA decay.
findings point to PKM2 and PTBP1 as new potential therapeutic targets to improve response of PDAC to chemotherapy
PTBP1 and PTBP2 impaired autoregulation of SRSF3 in oral squamous cell carcinoma cancer cells.
Results suggest that the role of polypyrimidine tract binding protein 1 (PTBP1) in tumorigenesis may be partly mediated by its regulation of cdc42 GTP-binding protein (CDC42) alternative splicing and CDC42-v2 might function as a tumor suppressor.
inactivation of both exosc9, which encodes a component of the RNA exosome, and ptbp1, which encodes an RNA-binding protein abundant in Xenopus embryonic skin, impairs embryonic Xenopus skin development.
Polypyrimidine tract binding protein prevents activity of an intronic regulatory element that promotes usage of a composite 3'-terminal exon
Study unveils an H19/PTBP1/sterol regulatory element-binding protein 1 feedforward amplifying signaling pathway to exacerbate the development of fatty liver.
In round spermatids, MRG15 colocalizes with splicing factors PTBP1 and PTBP2 at H3K36me3 sites between the exons and single intron of transition nuclear protein 2 (Tnp2). Thus, our results reveal that MRG15 is essential for pre-mRNA splicing during spermatogenesis and that epigenetic regulation of pre-mRNA splicing by histone modification could be useful to understand not only spermatogenesis but also, epigenetic disorder
This knockin Ptbp1 rescued a forebrain-specific, but not a pan-neuronal, Ptbp2 knockout, demonstrating both redundant and distinct roles for the proteins. Many developmentally regulated exons exhibited different sensitivities to PTBP1 and PTBP2.
Results indicate that heterogeneous nuclear ribonucleoprotein I (hnRNPI) plays a critical role in establishing neonatal immune adaptation and preventing colitis and colorectal cancer.
Thus, PTBP1 controls the activity of Pbx1 to suppress its neuronal transcriptional program prior to induction of neuronal progenitor cells development.
showed polypyrimidine tract binding protein (PTBP)-dependent alternative splicing of CaMKIIalpha transcripts in the lens
This may account for the tight correlation between Hps1 with Ptbp1 expression levels observed across mammalian tissues.
The expression levels of three splicing factors, ESRP1, PTB and SF2/ASF, are significantly altered during cardiac hypertrophy in mice.
Study reports that repression of a single RNA binding polypyrimidine-tract-binding (PTB) protein, which occurs during normal brain development via the action of miR-124, is sufficient to induce trans-differentiation of fibroblasts into functional neurons.
The polypyrimidine tract binding proteins PTBP1 and PTBP2 repressed Psd-95 (also known as Dlg4) exon 18 splicing, leading to premature translation termination and nonsense-mediated mRNA decay.
PTBP1 is not required for the earliest isovolumetric divisions and differentiation steps of the zygote up to the formation of the blastocyst.
RBM4 may synergize its effect on muscle cell-specific alternative splicing by down-regulating PTB expression and antagonizing the activity of PTB in exon selection
splicing repressors hnRNP A1 and A2, as well as the polypyrimidine-tract-binding protein PTB, contribute to control of pyruvate kinase isoform M1 and M2 expression
Data indicate that PTB is essential for early mouse development and ES cell proliferation.
Nucleocytoplasmic shuttling of polypyrimidine tract-binding protein is uncoupled from RNA export
PTB NES is a functionally important domain of this multifunctional protein that utilizes an unknown export receptor.
alternative splicing of brain-specific PTB has an important role in regulation of tissue-specific gene expression and thus in the functional activity of PTB in neuronal and non-neuronal cells
Polypyrimidine tract-binding protein (PTB) is necessary but not sufficient for regulation of tropomyosin splicing.
We conclude that expression of the PTB gene controls insulin production.
PTBP2, but not PTBP1, binds to a specific region of the Pgk2 3'-UTR.
Data report on a zebrafish maternal-effect mutant, brom bones, which is defective in the cytosolic Ca(2+) rise and subsequent egg activation events, including cortical granule exocytosis and cytoplasmic segregation [brom bones].
Two stretches of polypyrimidine tracts designated PPT1 and PPT2 which influence the IRES activity of cx55.5 protein were identified; deletion of PPT1 results in an appreciable decrease of the IRES activity
PTB1 is a splicing factor that influences alternative splicing and acts at the polypyrimidine tract.
Alternative splicing (AS) patterns as well as the expression of key flowering regulators were massively changed in a PTB1/2 level-dependent manner.
AtPTB1 and AtPTB2 are widely expressed in almost all tissues, with the highest expression levels in late-maturing and mature pollen grains, and are crucial for pollen germination. [AtPTB1]
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described.
57 kDa RNA-binding protein PPTB-1
, RNA-binding protein
, heterogeneous nuclear ribonucleoprotein I
, heterogeneous nuclear ribonucleoprotein polypeptide I
, hnRNP I
, polypyrimidine tract binding protein (heterogeneous nuclear ribonucleoprotein I)
, polypyrimidine tract-binding protein 1
, polypyrimidine tract binding protein 1
, hnrnp I
, hnRNP I-related RNA transport protein VgRBP60
, polypyrimidine tract-binding protein
, pyrimidine binding protein 1
, pyrimidine binding protein 2
, brom bones
, LOW QUALITY PROTEIN: polypyrimidine tract-binding protein 1