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PABPN1 encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. Additionally we are shipping Poly A Binding Protein Nuclear 1 Antibodies (35) and Poly A Binding Protein Nuclear 1 Proteins (6) and many more products for this protein.
We propose that the extensive binding of CircPABPN1 to HuR (show ELAVL1 ELISA Kits) prevents HuR (show ELAVL1 ELISA Kits) binding to PABPN1 mRNA and lowers PABPN1 translation, providing the first example of competition between a circRNA and its cognate mRNA for an RBP (show RBP4 ELISA Kits) that affects translation.
Whereas PABPN1 strongly increases the activity of its cognate poly(A) polymerase (show PAPOLA ELISA Kits) in vitro, Pab2 was unable to stimulate Pla1 (show POU2F3 ELISA Kits) to any significant extent.
The described is the mRNA degradation poly(A) tail exosome targeting (PAXT) connection, which comprises the ZFC3H1 Zn-knuckle protein as a central link between MTR4 and the nuclear poly(A)-binding protein PABPN1.
PABPN1 aggregates are able to trap TNNT3 pre-mRNA, driving it outside nuclear speckles, leading to an altered SC35 (show SRSF2 ELISA Kits)-mediated splicing.
The levels of these 6 cytokines were not altered in expPABPN1 carriers at a pre-symptomatic stage, suggesting that this group of cytokines is a potential biomarker for muscle weakness in OPMD. Correlation pattern of expression levels could be a novel measurer for disease state
Large cohort study demonstrated that in heterozygous and homozygous patients with oculopharyngeal muscular dystrophy, the mean age at diagnosis and the severity of the clinical symptoms correlate to the number of PABPN1 (GCN) repeats. Homozygous patients showed the worse phenotype, suggesting a gene-dose effect in addition to the repeat number expansion.
we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 and the poly(A)-specific RNase PARN (show PARN ELISA Kits).
Many ribozymes were assayed and validated, including four ribozymes targeting the transcript of a disease-causing gene (a mutant version of PABPN1).
Studied if the stability of the RNP (show RNPC3 ELISA Kits) domain of PABPN1 or domain swapping within the RNP (show RNPC3 ELISA Kits) domain may add to fibril formation.
This function is mediated by the concerted actions of the nuclear poly(A) binding protein PABPN1, poly(A) polymerase (PAP (show PAPOLA ELISA Kits)), and the nuclear exosome complex, a pathway we have named PABPN1 and PAP (show REG3A ELISA Kits)-mediated RNA decay (PPD (show HPD ELISA Kits))
PABPN1 measures the length of the tail and is responsible for disrupting the CPSF (show CPSF2 ELISA Kits)-poly(A) polymerase (show PAPOLA ELISA Kits) interaction.
Matrin 3 (MATR3 (show MATR3 ELISA Kits)) is a novel protein interactor of PABPN1. MATR3 (show MATR3 ELISA Kits) also binds and regulates the levels of long non-coding RNA (lncRNA) Neat1 and together with PABPN1 is required for normal paraspeckle function.
Expression levels of these cytokines were highly correlated in controls, but this correlation pattern was disrupted in OPMD. The levels of these 6 cytokines were not altered in expPABPN1 carriers at a pre-symptomatic stage, suggesting that this group of cytokines is a potential biomarker for muscle weakness in OPMD.
educed PABPN1 levels caused a consistent decline in distal PAS utilization in the 3'-UTR of a subset of OPMD-dysregulated genes. This alternative PAS utilization led to up-regulation of Atrogin-1, a key muscle atrophy regulator, but down regulation of proteasomal genes. Additionally reduced PABPN1 levels caused a reduction in proteasomal activity, and transition in MyHC isotope expression pattern in myofibers.
PABPN1 interacts with and is stabilized by heat shock protein 90 (show HSP90 ELISA Kits).
These findings demonstrate a role for PABPN1 in rescuing several cytopathological features of TDP-43 (show TARDBP ELISA Kits) proteinopathy by increasing the turnover of pathologic proteins.
the first step of the cleavage and polyadenylation reaction, mRNA cleavage, is affected in muscles expressing alanine-expanded PABPN1. We propose that impaired cleavage is an early defect in Oculopharyngeal muscular dystrophy.
These results suggest that PABPN1 levels regulate muscle cell aging and oculopharyngeal muscular dystrophy represents an accelerated muscle aging disorder.
tristetraprolin (show ZFP36 ELISA Kits) inhibits poly(A) tail synthesis by interacting with poly(A)-binding protein nuclear 1 in the nucleus to regulate expression of AU-rich element-containing mRNA
PABPN1 plays an essential role in myoblast proliferation and differentiation, suggesting that it is required for muscle regeneration and maintenance in vivo.
PABPN1 has a role in myogenesis
Poly(A) Binding Protein binds to uridylated oligo(A) tails and determines the length of U-extensions added by URT1.
PAB2 was partially retargeted to the nucleolus in the presence of TuMV VPg-Pro. In addition, the membrane association of PAB2 during TuMV infection resulted from the internalization of the host protein in 6K-VPg-Pro-induced vesicles.
Thus, Hsc70-3 and PABP2 are potentially integral components of the replicase complex and could have important roles to play in the regulation of potyviral RdRp functions.
This gene encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. The protein is required for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and controls the size of the poly(A) tail to about 250 nt. At steady-state, this protein is localized in the nucleus whereas a different poly(A) binding protein is localized in the cytoplasm. This gene contains a GCG trinucleotide repeat at the 5' end of the coding region, and expansion of this repeat from the normal 6 copies to 8-13 copies leads to autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Related pseudogenes have been identified on chromosomes 19 and X. Read-through transcription also exists between this gene and the neighboring upstream BCL2-like 2 (BCL2L2) gene.
poly(A) binding protein 2
, poly(A) binding protein II
, polyadenylate-binding protein 2
, nuclear poly(A)-binding protein 1
, poly(A)-binding protein 2
, poly(A)-binding protein II
, polyadenylate-binding nuclear protein 1