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anti-Human PTBP1 Antibodies:
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Human Polyclonal PTBP1 Primary Antibody for 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 for 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 for 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
Human Polyclonal PTBP1 Primary Antibody for IHC, WB - ABIN3022618
Wei, Dai, Zhou, He, Yao, Zhao, Guo, Yang: Oroxylin A activates PKM1/HNF4 alpha to induce hepatoma differentiation and block cancer progression. in Cell death & disease 2018
Study provides a novel mechanism that PTBP1 modulates Mena exon11a skipping, and indicates that PTBP1 depends on the level of Mena11a- to promote lung cancer cells migration and invasion.
PTBP1 expression correlates with disease progression, poor prognosis, and worse survival in patients with NMIBC. Downregulation of PTBP1 expression affects prosurvival features of bladder cancer cells and modulates AS of genes with relevance for bladder cancer, suggesting its role as an outcome-predictor in this disease.
PTBP1 enhances miR-101-guided AGO2 interaction with MCL1, thereby regulating miR-101-induced apoptosis and clonogenic cell survival inhibition in cells.
PTBP1 exerts these effects, in part, by regulating the phosphatase and tensin homolog-phosphatidylinositol-4,5-bisphosphate 3-kinase/protein kinase B (PTEN-PI3K/Akt) pathway and autophagy, and consequently alters cell growth and contributes to the invasion and metastasis.
PTB4 is a novel titin splicing regulator that counteracts the splice repressor activity of RBM20.
These results indicate that RBM20 and PTBP1 play a role in the actin filament functional organization mediated by FHOD3 isoforms and suggest their possible involvement in heart diseases.
Our results suggested that differential effects of MSCs on the invasion of cancer cells partially corresponded to PTBP1 expression in cancer cells and the maintenance of biological characteristics in MSCs, which insight could provide a theoretical basis for evaluating the safety of MSC application and PTBP1 targeting in cancer treatment.
PTBP1 and MATR3 co-bind and repress RNA processing within and around young LINEs
These results suggest that PTB interacts with the Enterovirus 71 internal ribosomal entry site, and positively regulates viral protein translation.
Knockdown of PTBP1 increases the expression of PTBP2 which also interacts with NOVA1, potentially preventing the association of NOVA1 with hTERT pre-mRNA.
The polypyrimidine tract binding protein is a monomer.
PTBP1 regulates the alternative splicing of genes involved in intracellular trafficking, such as EXOC7, to control the senescence-associated secretory phenotype, regulating inflammation driven cancer.
knockdown enhanced the sensitivity of drug-resistant colon cancer cells to vincristine and oxaliplatin through repression of glycolysis.
PTBP1 acts as a dominant repressor of ISCU mis-splicing in hereditary myopathy with lactic acidosis.
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.
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
A developmentally regulated spliced variant of PTBP1 is upregulated in experimental type 1 diabetic hearts.
In female cells with mutated polypyrimidine tract binding protein 1 (Ptbp1), differentiation fails to substantially upregulate mature Xist RNA because of a defect in Xist splicing...We conclude post-transcriptional control of Xist RNA splicing is an essential regulatory step of Xist induction
Interaction of PTBP1 with downstream intronic sequences can activate natural cassette exons by promoting productive docking of the spliceosomal U1 snRNP to a suboptimal 5' splice site. Ptbp1 promotes inclusion of the alternative exon 6 in Dtx2 mRNA. Activation of e6 depends on interaction between PTBP1 and U1.
data suggest that polypyrimidine tract binding protein 1 (PTBP1) contributes to spermatogenesis through regulation of spermatogonia proliferation
we found that the RNA-binding protein PTBP1 was needed for the progression of germinal center B cells through late S phase of the cell cycle and for affinity maturation
The authors show that PTBP1 directly represses miR-124 expression at the level of pri-miRNA processing.
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 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