PRMT1 Homogeneous Assay Kit
- Known as:
- PRMT1 Homogeneous Assay Kit
- Catalog number:
- 52054
- Product Quantity:
- 384 reactions
- Category:
- Peptides
- Supplier:
- BPS Bioscience
- Gene target:
- PRMT1 Homogeneous Assay Kit
Related genes to: PRMT1 Homogeneous Assay Kit
- Gene:
- PRMT1 NIH gene
- Name:
- protein arginine methyltransferase 1
- Previous symbol:
- HRMT1L2
- Synonyms:
- HCP1, ANM1
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1996-10-02
- Date modifiied:
- 2017-12-15
- Gene:
- PRMT9 NIH gene
- Name:
- protein arginine methyltransferase 9
- Previous symbol:
- PRMT10
- Synonyms:
- FLJ46629
- Chromosome:
- 4q31.23
- Locus Type:
- gene with protein product
- Date approved:
- 2009-05-15
- Date modifiied:
- 2015-09-07
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- Protein arginine methyltransferases (PRMTs) are a class of enzymes that mediate critical post-translational modifications through arginine methylation as epigenetic regulators. PRMTs have been shown to have a vast array of regulatory effects including in gene expression, signal transduction, and cellular proliferation. Dysregulation of PRMT activity has been seen in the progression of various cancers, including breast, lung, and colorectal cancer. Moreover, PRMT overexpression has been shown to correlate with poor patient prognosis. This review aims to explore the roles of the individual PRMTs in cancer and aims to highlight the latest and newest developments of PRMT inhibitors as emerging therapeutic strategies. Numerous preclinical and clinical studies have identified several novel compounds that effectively target PRMT activity and have shown significant therapeutic results. As such, this review aims to not only highlight the current research findings, but to also emphasize the significant need for future research on PRMTs as novel therapeutic targets in cancer. - Source: PubMed
Publication date: 2025/08/16
Kaganovski AdrianaSmith-Salzberg BayleShimshon Hadar KDraheim AndrewSpivak MarkSapir TzurielShifteh David - Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity. - Source: PubMed
Publication date: 2023/02/21
Li Alice Shi MingHomsi CharlesBonneil EricThibault PierreVerreault AlainVedadi Masoud - Arginine methylation is a post-translational modification involved in gene transcription, signalling pathways, DNA repair, RNA metabolism and splicing, among others, mechanisms that in protozoa parasites may be involved in pathogenicity-related events. This modification is performed by protein arginine methyltransferases (PRMTs), which according to their products are divided into three main types: type I yields monomethylarginine (MMA) and asymmetric dimethylarginine; type II produces MMA and symmetric dimethylarginine; whereas type III catalyses MMA only. Nine PRMTs (PRMT1 to PRMT9) have been characterized in humans, whereas in protozoa parasites, except for Giardia intestinalis, three to eight PRMTs have been identified, where in each group there are at least two enzymes belonging to type I, the majority with higher similarity to human PRMT1, and one of type II, related to human PRMT5. However, the information on the role of most of these enzymes in the parasites biology is limited so far. Here, current knowledge of PRMTs in protozoan parasites is reviewed; these enzymes participate in the cell growth, stress response, stage transitions and virulence of these microorganisms. Thus, PRMTs are attractive targets for developing new therapeutic strategies against these pathogens. - Source: PubMed
Publication date: 2021/12/06
Rodriguez Mario Alberto - To investigate the changes in the transcription of protein arginine methylation enzyme family genes in the dorsal root ganglia (DRG) following peripheral nerve injury in mice. - Source: PubMed
Xu Hua-LiXu Shi-YuanMo Kai - Signal transduction in response to stimuli relies on the generation of cascades of posttranslational modifications that promote protein-protein interactions and facilitate the assembly of distinct signaling complexes. Arginine methylation is one such modification, which is catalyzed by a family of nine protein arginine methyltransferases, or PRMTs. Elucidating the substrate specificity of each PRMT will promote a better understanding of which signaling networks these enzymes contribute to. Although many PRMT substrates have been identified, and their methylation sites mapped, the optimal target motif for each of the nine PRMTs has not been systematically addressed. Here we describe the use of Oriented Peptide Array Libraries (OPALs) to methodically dissect the preferred methylation motifs for three of these enzymes - PRMT1, CARM1 and PRMT9. In parallel, we show that an OPAL platform with a fixed methylarginine residue can be used to validate the methyl-specific and sequence-specific properties of antibodies that have been generated against different PRMT substrates, and can also be used to confirm the pan nature of some methylarginine-specific antibodies. - Source: PubMed
Publication date: 2016/06/24
Gayatri SitaramCowles Martis WVemulapalli VidyasiriCheng DonghangSun Zu-WenBedford Mark T