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Validated All-in-One™ qPCR Primer for PTBP1(NM_002819.4) Search again
Product ID:
HQP015525
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HNRNP-I, HNRNPI, HNRPI, PTB, PTB-1, PTB-T, PTB2, PTB3, PTB4, pPTB
Gene Description:
polypyrimidine tract binding protein 1
Target Gene Accession:
NM_002819.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- 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.
- chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein
- translation of some IRES-containing mRNAs is regulated by proteolytic cleavage of PTB during apoptosis
- resonance assignment and topology of the 2H, 13C, 15N labelled 29 kDa N-terminal fragment
- PTB has been identified as a component of the putative complex involved in regulating the stability of CD154 mRNA at late times of T cell activation.
- Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins and plays a role in spliceosome assembly
- unr and nPTB act as RNA chaperones by changing the structure of the IRES into one that permits translation initiation
- nucleo-cytoplasmic transport of PTB is regulated by the 3',5'-cAMP-dependent protein kinase (PKA)
- Strong upregulation of PTB expression in tumor cells of glial or primitive neuroectodermal origin suggests involvement of this protein in cellular transformation.
- The interactions of PTB-1 and PCBP1 with their cognate binding sites on the Bag-1 IRES disrupt many of the RNA-RNA interactions, and this creates a largely unstructured region of approximately 40 nucleotides that could permit ribosome binding.
- Data show that RNA recognition motifs (RRMs) 1 and 2 of polypyrimidine tract binding protein (PTB) contribute to RNA binding and that full-length PTB is monomeric, with an elongated structure consistent with a linear arrangement of RRMs.
- investigated the role of PTB for hepatitis C virus (HCV) translation, replication and chronic HCV infection; PTB inhibits HCV IRES-mediated translation but data do not indicate a significant role of PTB for HCV replication and chronic HCV infection
- upstream element in human papillomavirus type 16 interacted specifically with CstF-64, hnRNP C1/C2 & polypyrimidine tract binding protein, suggesting these factors were enhancing or regulating polyadenylation at the HPV-16 early polyadenylation signal
- solution structures of the four RNA binding domains (RBDs) of PTB; found that PTB is both a sequence-specific RNA binding protein with a preference for CU tracts and an RNA remodeler with an ability to bring separated pyrimidine tracts into proximity
- analysis of the splicing repressor domain in polypyrimidine tract-binding protein
- PTBP1 is a monomer.
- The structure of the two C-terminal RNA recognition motifs (RRM3 and RRM4) of PTB was studied.
- Small-angle X-ray scattering to determine the low-resolution structure of the entire PTB was used.
- Data showed that polypyrimidine tract binding protein PTB, a known IRES trans-acting factor or ITAF, is pivotal in regulating the apoptotic process by controlling IRES function.
- Obtained results do give insights into PTB's affinity for different RNA sequences. The low-energy conformations of the complexes provided information about the mechanism of binding. The analysis showed that binding is not RNA sequence-specific
- Identification of PSF, p54(nrb), PTB, and U1A as proteins specifically bound to the COX-2 polyadenylation signal upstream sequence elements .
- The results are consistent with a repressive mechanism in which cooperative binding of PTB to the PPT competes with binding of U2AF, thereby specifically blocking splicing of the alpha-actinin SM exon.
- Improved segmental isotope labeling methods for the NMR study of multidomain large proteins: application to RNP L.
- Under polypyrimidine tract binding protein-mediated repression, assembly was arrested at an A-like complex that was unable to transition to spliceosomal complexes.
- overexpression of polypyrimidine tract binding protein (PTB) induces HPV-16 late gene expression in cells transfected with subgenomic HPV-16 plasmids or with full-length HPV-16 genomes and in persistently HPV-16-infected cells.
- results provide a striking illustration of the importance of mRNA codon content in determining levels of PTB protein expression, even within cells of the natural host species
- PTB is not oncogenic and can either promote or antagonize a malignant trait dependent upon the specific intra-cellular environment
- in response to cellular activation in T cells and B cells, a PTB-containing stability complex forms that contains binding sites for Rab8A and cyclin D(2) transcripts and increases their mRNA half-lifes