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PTRF encodes a protein that enables the dissociation of paused ternary polymerase I transcription complexes from the 3' end of pre-rRNA transcripts. Additionally we are shipping PTRF Antibodies (56) and PTRF Kits (6) and many more products for this protein.
Showing 5 out of 6 products:
The expression of the PTRF protein was significantly weaker than that in the adjacent normal lung tissues using immunohistochemical staining. The findings revealed that miR187 promotes cell growth and invasion by targeting PTRF and miR187 may be a new prognostic factor for nonsmall cell lung cancer
A homozygous PTRF mutation was identified in patient-1. Congenital generalized lipodystrophy type 4 was caused by homozygous PTRF c.481-482insGTGA (p.Lys161Serfs*41) mutation in patient-2.
This study reports an unanticipated function of ROR1 (show ROR1 Proteins) as a scaffold of cavin-1 and caveolin-1 (show CAV1 Proteins), two essential structural components of caveolae.
Cavin-1 and cavin-2 (show SDPR Proteins) are strongly expressed within caveolae-like structures within liver sinusoidal endothelial cells of the hepatitis C-related cirrhotic liver and cavin-1 would play a critical role in regulating aspects of caveolin-1 (show CAV1 Proteins).
Rather than forming a single coat complex containing the three cavin family members, single-molecule analysis reveals an exquisite specificity of interactions between cavin1, cavin2 (show SDPR Proteins) and cavin3 (show PRKCDBP Proteins).
Our data support a role for PTRF/cavin-1, through caveolae formation, as an attenuator of the non-caveolar functionality of Cav1 (show CAV1 Proteins) in Gal3 (show LGALS3 Proteins)-Cav1 (show CAV1 Proteins) signalling and regulation of focal adhesion dynamics and cancer cell migration.
this study presents a novel mutation of PTRF from Saudi Arabia and our findings broaden the mutation spectrum of PTRF in the familial CGL4 phenotype.
cavin3 (show PRKCDBP Proteins) is recruited to the caveolae coat by cavin1 to interact with caveolin1 and regulate the duration time of caveolae at the plasma membrane.
The presence of caveolae as an anatomic structure is not sufficient to ensure their proper function in patient with PTRF mutation.
Using in silico and in vitro analysis we show that Cavin-1 is expressed in myogenic Rhabdomyosarcoma tumors and human and primary mouse RMS cultures. Cavin-1 or Cav-1 (show CAV1 Proteins) knockdown led to impairment of cell proliferation and migration.
these results suggested that the membrane dynamics in cell migration is affected by caveolae associated PTRF/cavin-1.
study demonstrates a critical role of cavin-1 in vascular structure and function, but the influences on arterial resistance cancel each other such that arterial blood pressure remains unaltered in homeostatic conditions
lipid mobilization in cultured adipocytes to induce lipid droplet shrinkage led to biphasic response of cavin-1 with ultimate loss of expression of cavin-1 by protein degradation.
A Western-type diet in apo (show C9orf3 Proteins)-E2 knock-in mice produced 3 groups of obese mice with PTRF expression correlating with glucose tolerance: normal, hyperinsulinemic glucose-tolerant, or impaired. PTRF compromised adipocyte differentiation of 3T3-L1 cells.
Adipocytes from cavin-1-null mice are markedly dysfunctional exhibiting decreased insulin (show INS Proteins)-dependent glucose uptake, fatty acid uptake, and lipolysis.
PTRF is a crucial regulator of TLR4 (show TLR4 Proteins) signaling in the development of sepsis.
an important role for Cavin1 in lung homeostasis
Cavin-1 is critical for detrusor caveolae and for overall contractility and structure of the urinary bladder.
Cavin-1 modulates cellular polarization, and the subcellular localization of Rac1 and caveolin-1 (show CAV1 Proteins) in migrating cells as well as PKCalpha (show PKCa Proteins) caveola recruitment.
Double-immunogold labeling showed that the caveolae-shaping molecule PTRF/cavin 1 behaved similarly and that syndapin II (show PACSIN2 Proteins) and PTRF/cavin 1 colocalized.
This gene encodes a protein that enables the dissociation of paused ternary polymerase I transcription complexes from the 3' end of pre-rRNA transcripts. This protein regulates rRNA transcription by promoting the dissociation of transcription complexes and the reinitiation of polymerase I on nascent rRNA transcripts. This protein also localizes to caveolae at the plasma membrane and is thought to play a critical role in the formation of caveolae and the stabilization of caveolins. This protein translocates from caveolae to the cytoplasm after insulin stimulation. Caveolae contain truncated forms of this protein and may be the site of phosphorylation-dependent proteolysis. This protein is also thought to modify lipid metabolism and insulin-regulated gene expression. Mutations in this gene result in a disorder characterized by generalized lipodystrophy and muscular dystrophy.
polymerase I and transcript release factor
, leucine zipper protein
, leucine-zipper protein
, polymerase I and transcript release factor-like
, RNA polymerase I and transcript release factor
, TTF-I interacting peptide 12