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Human Polyclonal PTBP2 Primary Antibody for ELISA, WB - ABIN566177
Rolland, Evrard, Guitton, Lavigne, Calvel, Couvet, Jégou, Pineau: Two-dimensional fluorescence difference gel electrophoresis analysis of spermatogenesis in the rat. in Journal of proteome research 2007
Show all 6 Pubmed References
Human Monoclonal PTBP2 Primary Antibody for ELISA, WB - ABIN566178
Xue, Zhou, Wu, Zhu, Ji, Kwon, Zhang, Yeo, Black, Sun, Fu, Zhang: Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping. in Molecular cell 2010
Show all 2 Pubmed References
Cow (Bovine) Polyclonal PTBP2 Primary Antibody for WB - ABIN2776545
Tateiwa, Gotoh, Ichikawa, Kikuchi, Yoshimura: Molecular cloning and characterization of human PTB-like protein: a possible retinal autoantigen of cancer-associated retinopathy. in Journal of neuroimmunology 2001
Human Polyclonal PTBP2 Primary Antibody for ELISA - ABIN548022
Boutz, Stoilov, Li, Lin, Chawla, Ostrow, Shiue, Ares, Black: A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons. in Genes & development 2007
It has been established that PTBP1 and PTBP2 are members of a family of cryptic exon repressors.
PTBP1 and PTBP2 impaired autoregulation of SRSF3 in oral squamous cell carcinoma cancer cells.
Data show that polypyrimidine tract-binding proteins nPTB and ROD1 interact with mitochondrial tRNA(Thr) in the cytoplasm outside of mitochondria.
In T98G glioma cells, the level of sumoylated PTBP2 was reduced compared to that of normal brain cells. Overall, this study shows that PTBP2 is posttranslationally modified by SUMO1.
MALAT1 binds to SFPQ releasing PTBP2 from the SFPQ/PTBP2 complex, the increased SFPQ-detached PTBP2 promotes cell proliferation and migration in colorectal cancer.
Defining the multifunctional roles of PTB will contribute to the understanding of key regulatory events in gene expression.
Changes in miR-223/PTBP2 pathway could contribute of abnormal splicing in chronic myeloid leukemia.
Regulation of the mutually exclusive exons 8a and 8 in the CaV1.2 calcium channel transcript by polypyrimidine tract-binding protein.
present fluorescence, NMR, and in vivo splicing data in support of a role of PTB in inducing RNA loops. We show that the RNA recognition motifs (RRMs) 3 and 4 of PTB can bind two distant pyrimidine tracts and bring their 5' and 3' ends in close proximity
The nPTB proximal promoter, although rich in G+C content and presenting putative binding sites for the transcription factors Sp1, NF-1, NF-kB and Oct-1, lacks a typical TATA box.
Study shows that PTB can function as an anti-repressor molecule to counteract the splicing inhibitory activity of SRp30c.
splicing regulation by Ptbp2 is critical for germ cell communication with Sertoli cells
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.
Ptbp2 is an essential factor in heat stress-induced sperm cell injury and non-obstructive azoospermia.
Ptbp2 ablation results in germ cell loss due to increased apoptosis of meiotic spermatocytes and postmeiotic arrest of spermatid differentiation.
These results define a new genetic regulatory program, where PTBP2 acts to temporarily repress expression of adult protein isoforms until the final maturation of the neuron.
Thus, Ptbp2 inhibition of a discrete set of adult neuronal exons underlies early brain development prior to neuronal differentiation and is essential for postnatal survival.
The expression of PSD-95 during early neural development is controlled at the RNA level by two PTB proteins whose sequential downregulation is necessary for synapse maturation.
The present study provides evidence that alternative neuronal nPTB and Fox-1/Fox-2 isoforms are also produced in lenses
Reduction of PTBP2 levels led to decreases in 7 of 10 of the mRNAs, to the repression of alternative splicing of introns, and to reductions in specific miRNAs.
knock-down inhibits immunoglobulin class-switch recombination
The predominant expression of REST4, HuB/C/D and nPTB in post-mitotic fiber cells, together with miR-124 expression in vertebrate lenses, was shown.
PTBP2 is a trans-acting factor that helps to stabilize Pgk2 mRNA in male mouse germ cells.
The post-transcriptional switch from PTB to nPTB controls a widespread alternative splicing program during neuronal development.
PTBP2 was identified as a brain-expressed protein that interacts with the paraneoplastic target antigen Nova1 by yeast 2-hybrid, in vivo co-IP and co-localization in neurons. Functionally, the proteins antagonize each other in splicing assays.
Two stretches of polypyrimidine tracts designated PPT1 and PPT2 which influence the IRES activity of cx55.5 protein were identified; deletion of PPT2 results in a complete loss of the IRES activity
The protein encoded by this gene binds to the intronic cluster of RNA regulatory elements, downstream control sequence (DCS). It is implicated in controlling the assembly of other splicing-regulatory proteins. This protein is very similar to the polypyrimidine tract binding protein but it is expressed primarily in the brain.
, neural polypyrimidine tract binding protein
, neural polypyrimidine tract-binding protein
, neurally-enriched homolog of PTB
, polypyrimidine tract-binding protein 2
, splicing regulator
, RRM-type RNA-binding protein brPTB
, brain-enriched PTB
, brain-enriched polypyrimidine tract-binding protein
, polypyrimidine tract binding protein 2
, polypyrimidine tract-binding protein 2-like
, uncharacterized protein LOC541437