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anti-Human CARM1 Anticorps:
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Human Polyclonal CARM1 Primary Antibody pour ICC, IF - ABIN152377
Harrison, Tang, Dowhan: Protein arginine methyltransferase 6 regulates multiple aspects of gene expression. dans Nucleic acids research 2010
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Human Monoclonal CARM1 Primary Antibody pour ICC, FACS - ABIN969002
Fauquier, Duboé, Joré, Trouche, Vandel: Dual role of the arginine methyltransferase CARM1 in the regulation of c-Fos target genes. dans FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2008
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Human Polyclonal CARM1 Primary Antibody pour IF (p), IHC (p) - ABIN763061
Wang, Cui, Wen, Guo, Zhang, Chen: Cisplatin induces HepG2 cell cycle arrest through targeting specific long noncoding RNAs and the p53 signaling pathway. dans Oncology letters 2017
Human Polyclonal CARM1 Primary Antibody pour WB - ABIN4287938
Herrmann, Pably, Eckerich, Bedford, Fackelmayer: Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family. dans Journal of cell science 2009
Human Polyclonal CARM1 Primary Antibody pour WB - ABIN2668761
Mann, Cortez, Vadlamudi: PELP1 oncogenic functions involve CARM1 regulation. dans Carcinogenesis 2013
Human Monoclonal CARM1 Primary Antibody pour IP, WB - ABIN6718874
Wu, Li, Li, Ti, Zhao, Si, Mei, Zhao, Fu, Han: LRP16 integrates into NF-κB transcriptional complex and is required for its functional activation. dans PLoS ONE 2011
Data suggest that targeting coactivator associated arginine methyltransferase 1 (CARM1) may be an effective therapeutic
CARM1-mediated asymmetric methylation of PRMT5 is critical for its dimerization and methyltransferase activity leading to the repression of gamma-globin expression.
CARM1 methylates PKM2 at arginines 445 and 447, which enhances PKM2 tetramer formation. Consequently, Carm1 knockout cells exhibit significant survival advantages over WT cells when extracellular serine is limited, likely due to their enhanced de novo serine synthesis capacity. Altogether, we identified CARM1 as an important regulator of glucose metabolism and serine synthesis.
CARM1 is a p53 responsive gene. p53 could suppress CARM1 promoter-driven luciferase expression.
Consistent with its role in transcriptional activation, JMJD6 is required for estrogen/ERalpha-induced breast cancer cell growth and tumorigenesis, via modulation of recruitment of CARM1/MED12 co-activator complex.
N-terminal EVH1 domain of CARM1 is necessary and sufficient for substrate recognition and is required for methylation of most CARM1 substrates.
SKP2 promotes HCC progression and its nuclear functions of autophagy induction with CARM1 and AMPK, which may provide a potential target for HCC therapy.
The Overexpression of CARM1 Promotes Human Osteosarcoma Cell Proliferation through the pGSK3beta/beta-Catenin/cyclinD1 Signaling Pathway
The CARM1-PKM2 axis serves as a metabolic reprogramming mechanism in tumorigenesis.
Arginine (di)methylated human leukocyte antigen class I peptides, which are asymmetrically dimethylated, most likely by CARM1, are favorably presented by HLA-B*07.
Estrogen receptor recruits steroid receptor coactivator-3 primary coactivator and secondary coactivators, p300/CBP and CARM1 to regulate genetic transcription.
Arginine methylation of MDH1 by CARM1 regulates cellular redox homeostasis and suppresses glutamine metabolism of pancreatic cancer.
Here, the crystal structures of human CARM1 with the S-adenosylmethione (SAM) mimic sinefungin and three different peptide sequences from histone H3 and PABP1 are presented, with both nonmethylated and singly methylated arginine residues exemplified.
CARM1 associates with major nonsense-mediated mRNA decay factor UPF1 and promotes its occupancy on premature terminating codon-containing transcripts in spinal muscular atrophy.
Monitoring of the CARM1-dependent production of monomethylated and dimethylated peptides over time by self-assembled monolayer and matrix-assisted laser desorption ionization mass spectrometry revealed that methylation by CARM1 is distributive.
no obvious association of CARM1 isoform expression and clinical correlates in breast cancer
disruption of CARM1 enhances the nuclear retention of mRNAs containing IRAlus
Data indicate that coactivator-associated arginine methyltransferase 1 (CARM1) regulates neural differentiation through Nanog homeobox protein and microRNA miR92a.
Like insulin, CARM1 overexpression increased CDK2 and CDK4 expression. In addition, CARM1 knockdown reduced the number of insulin-induced G2/M phase cells
a noncoding variant in the CARM1-promoter functions as a regulator of gene transcription and homocysteine levels
our data demonstrate that CARM1 is required for transcriptional activation of a subset of RA target genes, and we uncover changes in the recruitment of Suz12 and the epigenetic H3K27me3 and H3K27ac marks at gene regulatory regions for CRABP2 and NR2F1 during RA-induced differentiation.
The Carm1 is a specific substrate of p38gamma/MAPK12 and that phosphorylation of Carm1 prevents its nuclear translocation.
CARM1 accumulates in nuclear granules at the 2- to 4-cell stage transition in the mouse embryo, with the majority corresponding to paraspeckles. The paraspeckle component Neat1 and its partner p54nrb are required for CARM1's association with paraspeckles and for H3R26 methylation.
High nuclear Carm1 levels negatively impact the p300*ACT*CREMtau axis during late stages of spermiogenesis.
CARM1 gene expression was repressed by p53 in 3T3L1 preadipocytes when activated with Nutlin-3a treatment. Ectopic CARM1 overexpression could rescue inhibitory effect of p53 on adipogenesis. p53 and CARM1 showed antagonistic regulatory influence on PPAR-gamma expression. p53-mediated suppression of adipogenesis could be partly via repression of CARM1 expression.
Study shows that peripheral nerve injury induced the upregulation of the mRNA and protein expression of coactivator-associated arginine methyltransferase 1 (CARM1) in the injured dorsal root ganglion. Findings suggest that CARM1 may serve as a promising therapeutic target for neuropathic pain treatment in clinical applications.
PRMT activity is selectively augmented during the initial activation of exercise-induced skeletal muscle remodeling in vivo.
C9orf72 acts by promoting the lysosomal degradation of coactivator-associated arginine methyltransferase 1 (CARM1), which in turn regulates autophagy-lysosomal functions and lipid metabolism.
the present study increases our understanding of PRMT1, -4, and -5 biology during the plasticity of skeletal muscle development. Our results provide evidence for a role of PRMT1, via a mitochondrially mediated mechanism, in driving the muscle differentiation program.
Study describes peptide-based transition state mimics that form stable complexes with CARM1 resulting in high-resolution co-crystal structures. The findings provide an exciting approach to understanding protein arginine methyltransferase (PRMT) substrate recognition and the regulation of arginine methylation.
CARM1 promotes EZH2-mediated silencing of EZH2/BAF155 target tumor suppressor genes by methylating BAF155.
These observations demonstrate that oxidative stress destabilizes PRMT4 via GSK-3beta signaling to impede lung epithelial cell migration that may hinder the lung repair and regeneration process.
AMPK deficiency results in nuclear CARM1 decrease mediated in part by SKP2, contributing to autophagy dysfunction in the aged heart.
Study identifies CARM1, which methylates histone H3 at arginine 26 (H3R26), as an upstream regulator of Sox21 expression. These results indicate that heterogeneity in gene expression patterns biases cell fate in the mouse embryo as early as the 4-cell stage.
findings demonstrate that CARM1-dependent histone arginine methylation is a crucial nuclear event in autophagy, and identify a new signalling axis of AMPK-SKP2-CARM1 in the regulation of autophagy induction after nutrient starvation
CARM1 haploinsufficiency impairs transdifferentiation and wound healing in a mouse model.
PRMT4 might be a key regulator of high-glucose-induced insulin secretion from pancreatic beta cells via H3R17 methylation.
Data show that the methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1; PRMT4) methylated Notch intracellular domain (NICD) at five conserved arginine residues.
we identify BAF155 as a substrate for arginine methyltransferase CARM1.
a combinatorial role of PRMT4/CARM1 and PRMT5 for proper myogenesis in zebrafish
Protein arginine N-methyltransferases, such as CARM1, catalyze the transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine. Protein arginine methylation has been implicated in signal transduction, metabolism of nascent pre-RNA, and transcriptional activation (Frankel et al., 2002
histone-arginine methyltransferase CARM1
, protein arginine N-methyltransferase 4
, coactivator-associated arginine methyltransferase 1
, protein arginine methyltransferase