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histone H3K9 acetyltransferase PCAF plays a critical role in osteogenic differentiation of mesenchymal stem cells.
cancer associated fibroblasts (CAFs) promoted hepatocellular cancer (HCC) growth via IL-6/STAT3/AKT pathway and TIMP-1 over-expression driven by IL-6/STAT3 pathway in HCC cells brought in more CAFs through activating liver fibroblasts.
These results uncover p300 (show EP300 Proteins) as a direct target of mTORC1 and suggest that the mTORC1-p300 (show EP300 Proteins) pathway plays a pivotal role in cell metabolism by coordinately controlling cell anabolism and catabolism
TNF-alpha (show TNF Proteins) and LPS (show IRF6 Proteins) promoted the interaction between MKL1 and PCAF.
PCAF is a novel modulator of autophagy in hepatocellular carcinoma.
a mechanism of transcriptional regulation mediated by p27 (show PAK2 Proteins), Pax5 (show PAX5 Proteins), and PCAF
The studies identify a P/CAF-PAX3 (show PAX3 Proteins)-FOXO1 (show FOXO1 Proteins) signalling node that promotes oncogenesis and may contribute to MyoD (show MYOD1 Proteins) dysfunction in Alveolar rhabdomyosarcoma (ARMS).
results strongly support our hypothesis that PCAF is induced and activated by ATRA, and the subsequent acetylation of PCAF substrates promotes granulocytic differentiation in leukemia cells
Our findings demonstrated a novel epigenetic mechanism of IL-10 (show IL10 Proteins) dysregulation in inflammatory bowel disease. Down-regulation of KAT2B may disrupt the innate and adaptive inflammatory responses due to the suppression of this crucial anti-inflammatory cytokine.
Acetyltransferase p300/CBP-associated factor (PCAF) interacts with and acetylates HOXB9 (show HOXB9 Proteins) both in vivo and in vitro.
These results uncover p300 (show NOTCH1 Proteins) as a direct target of mTORC1 and suggest that the mTORC1-p300 (show NOTCH1 Proteins) pathway plays a pivotal role in cell metabolism by coordinately controlling cell anabolism and catabolism
The epigenetic factor PCAF regulates vascular inflammation and is essential for intimal hyperplasia development.
This study demonstrated that pcaf increase in skeletal muscle in muscle atrophy.
Treatment with a pan-acetylase inhibitor, anacardic acid, reduced the binding affinity of p300 (show NOTCH1 Proteins) and PCAF to the NKX2.5 (show NKX2-5 Proteins), beta-MHC (show MYH7 Proteins), Cx43 (show GJA1 Proteins) promoters and attenuated H3K9 hyperacetylation.
Gcn5 (show KAT2A Proteins) and PCAF repress IFN-beta (show IFNB1 Proteins) production in an enzymatic activity-independent and non-transcriptional manner: by inhibiting the innate immune signaling kinase TBK1 (show TBK1 Proteins) in the cytoplasm.
PCAF acetylates two lysine residues K328 and K450 in PGC-1alpha. PCAF in the obese mouse liver greatly represses gluconeogenic enzyme activation and glucose production and improves glucose homeostasis and insulin (show INS Proteins) sensitivity.
Study reveals that Gcn5 (show KAT2A Proteins)/PCAF facilitate adipogenesis through regulation of PPARgamma (show PPARG Proteins) expression and regulate brown adipogenesis by influencing Prdm16 (show PRDM16 Proteins) expression.
KLF10, functions as a toggle to integrate antagonistic signals regulating FOXP3 (show FOXP3 Proteins) via Sin3-HDAC (show HDAC3 Proteins)/PCAF pathway and, thus, immune activation.
PCAF is necessary for axonal regeneration and also promotes regeneration after spinal cord injury.
CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation, including c-jun and the adenoviral oncoprotein E1A. The protein encoded by this gene associates with p300/CBP. It has in vitro and in vivo binding activity with CBP and p300, and competes with E1A for binding sites in p300/CBP. It has histone acetyl transferase activity with core histones and nucleosome core particles, indicating that this protein plays a direct role in transcriptional regulation.
, histone acetyltransferase KAT2B
, CREBBP-associated factor
, histone acetylase PCAF
, histone acetyltransferase PCAF
, lysine acetyltransferase 2B
, K(lysine) acetyltransferase 2B