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PRMT1 encodes a member of the protein arginine N-methyltransferase (PRMT) family. Additionally we are shipping PRMT1 Antibodies (146) and and many more products for this protein.
Showing 10 out of 31 products:
Human PRMT1 Protein expressed in HEK-293 Cells - ABIN2729657
Tikhanovich, Kuravi, Artigues, Villar, Dorko, Nawabi, Roberts, Weinman: Dynamic Arginine Methylation of Tumor Necrosis Factor (TNF) Receptor-associated Factor 6 Regulates Toll-like Receptor Signaling. in The Journal of biological chemistry 2015
Important roles of PRMT1 in progression of gastric cancer. Given the dual functions of PRMT1, it is as a potential drug target of gastric cancer with extreme caution.
Mitochondrial Ca(2 (show CA2 Proteins)+) uptake is controlled by protein arginine methyl transferase 1 that asymmetrically methylates MICU1 (show MICU1 Proteins), resulting in decreased Ca(2 (show CA2 Proteins)+) sensitivity. UCP2 (show UCP2 Proteins)/3 normalize Ca(2 (show CA2 Proteins)+) sensitivity of methylated MICU1 (show MICU1 Proteins) and, thus, re-establish mitochondrial Ca(2 (show CA2 Proteins)+) uptake activity.
High-PRMT1 expression is associated with resistance to cetuximab in triple-negative breast cancer.
a significant role for PRMT1 in HCC (show FAM126A Proteins) progression and metastasis in vitro and in vivo via STAT3 (show STAT3 Proteins) signalling pathway activation. PRMT1 may be a potential novel prognostic biomarker and new therapeutic target for hepatocellular carcinoma.
High PRMT1 expression is associated with head and neck and oral cancer.
TRIM48 Promotes ASK1 (show MAP3K5 Proteins) Activation and Cell Death through Ubiquitination-Dependent Degradation of the ASK1 (show MAP3K5 Proteins)-Negative Regulator PRMT1
data collectively suggest that silencing of PRMT1 exerts anti-catabolic and anti-inflammatory effects on IL-1beta (show IL1B Proteins)-induced chondrocytes via suppressing the Gli-1 (show GLI1 Proteins) mediated Hedgehog (show SHH Proteins) signaling pathway, indicating that PRMT1 plays a critical role in OA development and serves as a promising therapeutic target for OA.
Deacetylation on both K200 and K205 by Sirtuin 1 (Sirt1 (show SIRT1 Proteins)) and acetylation of p300 (EP300 (show EP300 Proteins)) on K205 collaboratively prepare the motif for SCF (show KITLG Proteins)(Fbxl17 (show FBXL17 Proteins)) binding thereby triggering PRMT1 protein degradation.
PRMT1 has a role in regulating MYCN (show MYCN Proteins) in neuroblastoma (show ARHGEF16 Proteins)
Analysis of deletion constructs of SERBP1 (show SERBP1 Proteins) showed that the C-terminal third of the SERBP1 (show SERBP1 Proteins) protein, which contains one of its two substrate sites for protein arginine N-methyltransferase 1 (PRMT1), is necessary and sufficient for it to interact with RACK1 (show GNB2L1 Proteins)
prmt8 (show PRMT8 Proteins) 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 (show PTH Proteins) (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.
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.
lipotoxicity-induced PRMT1 expression promotes endoplasmic reticulum stress-mediated mesangial cell apoptosis.
PRMT1 is an arginine methyltransferase involved in a variety of cell functions. Here the authors delete PRMT1 specifically in mature B cells to show the importance of arginine methylation for B cell proliferation, differentiation and survival, and thereby for humoral immunity.
Collectively, this study firstly demonstrated that PRMT1 exert podocyte-injury effects in mouse glomerulus through Ang (show ANG Proteins) /ERK (show EPHB2 Proteins) pathway, which reveals a potential therapeutic target for DN.
PRMT1 inhibition prevents gastric cancer progression by downregulating eIF4E (show EIF4E Proteins) and targeting type II PRMT5 (show PRMT5 Proteins).
Low Prmt1 expression is associated with osteosarcoma.
Collectively, the authors propose that Prmt1-dependent facilitation of KCNQ (show KCNQ1 Proteins)-phosphatidylinositol-4,5-bisphosphate interaction underlies the positive regulation of KCNQ (show KCNQ1 Proteins) 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 (show BTG2 Proteins)-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 (show MYC Proteins) binding to acetyltransferase p300 (show NOTCH1 Proteins) in myeloid cells; Prmt1 inhibition decreases p300 (show NOTCH1 Proteins) recruitment to c-Myc (show MYC Proteins) target promoters and increased Hdac1 (show HDAC1 Proteins) recruitment. [Prmt1, protein arginine N-methyltransferase 1; c-Myc (show MYC Proteins) = Proto-Oncogene (show RAB1A Proteins) Proteins c-myc (show MYC Proteins); Hdac1 (show HDAC1 Proteins) = histone deacetylase 1 (show HDAC1 Proteins)]
PRMT1-dependent regulation of macrophage PPARgamma (show PPARG Proteins) expression contributes to the infection susceptibility in PRMT1 knock-out mice
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