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PRMT1 encodes a member of the protein arginine N-methyltransferase (PRMT) family. Zusätzlich bieten wir Ihnen PRMT1 Proteine (36) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal PRMT1 Primary Antibody für EIA, WB - ABIN356520
Zhang, Zhou, Cheng: Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. in The EMBO journal 2000
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Human Polyclonal PRMT1 Primary Antibody für EIA, IHC (p) - ABIN356519
Scorilas, Black, Talieri, Diamandis: Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene. in Biochemical and biophysical research communications 2000
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Cow (Bovine) Polyclonal PRMT1 Primary Antibody für IHC, WB - ABIN2778664
Adams, Wang, Xia, Morales, Lu, Donehower, Bochar, Elledge, Carpenter: 53BP1 oligomerization is independent of its methylation by PRMT1. in Cell cycle (Georgetown, Tex.) 2005
Human Polyclonal PRMT1 Primary Antibody für IHC (p), IP - ABIN151674
Fisk, Zurita-Lopez, Sayegh, Tomasello, Clarke, Read: TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei. in Eukaryotic cell 2010
Our data suggest that miR (zeige MLXIP Antikörper)-19a and PRMT1 might be novel indicators of asthma and present new disease-specific therapeutic targets to reduce airway wall remodeling and inflammation in asthmatic patients
The PRMT1 active site residues, Met48 and His293, have been determined to play a key role in dictating product specificity, as: (1) the single mutation of Met48 to Phe enabled PRMT1 to generate MMA, ADMA, and a limited amount of SDMA; (2) the single mutation of His293 to Ser (zeige SIGLEC1 Antikörper) formed the expected MMA and ADMA products only; (3) the double mutant H293S-M48F-PRMT1 produced SMDA as the major product with limit amount of SDMA.
This article reviews the current literature from research showing interdependent association between cav1 (zeige CAV1 Antikörper)-PRMT1-SIRT1 (zeige SIRT1 Antikörper) to the outcomes of experimental and clinical research aiming to preserve endothelial function with gene- or pharmaco-therapy. [review]
Increase in HLAB expression was concomitant with increase in HIF-1alpha (zeige HIF1A Antikörper) and decrease in PRMT1 levels.
Low expression of PRMT1 is associated with low chemosensitivity in gastric cancer.
PRMT1 is overexpressed in human melanoma, and may regulate tumor growth and metastasis via targeting ALCAM (zeige ALCAM Antikörper).
Protein arginine N-methyltransferase 1 expression was found to be significantly upregulated in hepatocellular carcinoma cell lines and clinical tissues.
FAM98A, whose physiological function is unknown, was arginine-methylated by PRMT1.
PRMT1 promoted the methylation of Gli1 (zeige GLI1 Antikörper).
The oncogenic roles of PRMT1 in the progression of ESCC.
prmt8 (zeige PRMT8 Antikörper) may play important roles non-overlapping with prmt1 in embryonic and neural development depending on its specific N-terminus.
prmt1 gene is actively and ubiquitously expressed at both RNA and protein levels at the early developmental stages of zebrafish.
PRMT1 functions transiently as a coactivator in thyroid hormone (zeige PTH Antikörper) (T3) receptor (TR)-mediated transcription by enhancing TR-T3 response element binding and further suggest that PRMT1 has tissue-specific roles in regulating the rate of metamorphosis.
Results suggest that part of the type I arginine methyltransferases in brains, mainly PRMT1, are sequestered in an inactive form as they associated with membranes or large subcellular complexes.
Collectively, the authors propose that Prmt1-dependent facilitation of KCNQ (zeige KCNQ1 Antikörper)-phosphatidylinositol-4,5-bisphosphate interaction underlies the positive regulation of KCNQ (zeige KCNQ1 Antikörper) activity by arginine methylation, which may serve as a key target for prevention of neuronal hyperexcitability and seizures.
Results identify a key molecular mechanism by which the BTG2 (zeige BTG2 Antikörper)-PRMT1 module regulates pre-B cell differentiation and inhibits pre-B cell leukemogenesis.
Data, including data from studies in cells from knockout mice, suggest that Prmt1 activity was necessary for c-Myc (zeige MYC Antikörper) binding to acetyltransferase p300 (zeige NOTCH1 Antikörper) in myeloid cells; Prmt1 inhibition decreases p300 (zeige NOTCH1 Antikörper) recruitment to c-Myc (zeige MYC Antikörper) target promoters and increased Hdac1 (zeige HDAC1 Antikörper) recruitment. [Prmt1, protein arginine N-methyltransferase 1; c-Myc (zeige MYC Antikörper) = Proto-Oncogene (zeige RAB1A Antikörper) Proteins c-myc (zeige MYC Antikörper); Hdac1 (zeige HDAC1 Antikörper) = histone deacetylase 1 (zeige HDAC1 Antikörper)]
PRMT1-dependent regulation of macrophage PPARgamma (zeige PPARG Antikörper) expression contributes to the infection susceptibility in PRMT1 knock-out mice
These findings suggest that arginine methylation by PRMT1 regulates muscle stem cell fate through the Eya1 (zeige EYA1 Antikörper)/Six1 (zeige SIX1 Antikörper)/MyoD (zeige MYOD1 Antikörper) axis.
PRMT1 is necessary for lymphocyte functions in vivo.
The Protein arginine methyltransferase 1 (PRMT1) is involved in multiple cellular functions including proliferation and differentiation and PRMT1 is important for embryonic vascular formation.
A time-dependent decrease in serum and tissue ADMA and increase in mRNA expression of DDAH-1 and PRMT-1 as well as higher rates of mRNA expression of CAT-1 and lower rates of CAT-2A and CAT-2B were found after 8-week MCD diet.
PRMT1 is required for CNS development, especially for oligodendrocyte maturation processes
Pharmacological inhibition of KDM4C (zeige KDM4C Antikörper)/PRMT1 suppresses transcription and transformation ability of MLL (zeige MLL Antikörper) fusions
This gene encodes a member of the protein arginine N-methyltransferase (PRMT) family. Post-translational modification of target proteins by PRMTs plays an important regulatory role in many biological processes, whereby PRMTs methylate arginine residues by transferring methyl groups from S-adenosyl-L-methionine to terminal guanidino nitrogen atoms. The encoded protein is a type I PRMT and is responsible for the majority of cellular arginine methylation activity. Increased expression of this gene may play a role in many types of cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 5.
protein arginine N-methyltransferase 1
, protein arginine methyltransferase 1
, protein arginine N-methyltransferase
, HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 2
, heterogeneous nuclear ribonucleoprotein methyltransferase 1-like 2
, histone-arginine N-methyltransferase PRMT1
, interferon receptor 1-bound protein 4
, HMT1 hnRNP methyltransferase-like 2
, histone-arginine N-methyltransferase PRMT1-A
, protein arginine N-methyltransferase 1-A
, heterogeneous nuclear ribonucleoproteins methyltransferase-like 2
, arginine N-methyltransferase 1