PRMT4 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
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Primary Accession | Q86X55 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 65854 Da |
Gene ID | 10498 |
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Other Names | Histone-arginine methyltransferase CARM1, 211-, Coactivator-associated arginine methyltransferase 1, Protein arginine N-methyltransferase 4, CARM1, PRMT4 |
Target/Specificity | This PRMT4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human PRMT4. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | PRMT4 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CARM1 |
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Synonyms | PRMT4 |
Function | Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability (PubMed:12237300, PubMed:16497732, PubMed:19405910). Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling (PubMed:12237300, PubMed:16497732, PubMed:19405910). During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription (By similarity). During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C (By similarity). During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B (By similarity). Acts as a coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue (By similarity). Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors (By similarity). Also seems to be involved in p53/TP53 transcriptional activation (By similarity). Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation (PubMed:15731352). Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA- stabilizing properties and the half-life of their target mRNAs (By similarity). Acts as a transcriptional coactivator of ACACA/acetyl-CoA carboxylase by enriching H3R17 methylation at its promoter, thereby positively regulating fatty acid synthesis (By similarity). Independently of its methyltransferase activity, involved in replication fork progression: promotes PARP1 recruitment to replication forks, leading to poly-ADP-ribosylation of chromatin at replication forks and reduced fork speed (PubMed:33412112). |
Cellular Location | Nucleus. Cytoplasm. Chromosome. Note=Mainly nuclear during the G1, S and G2 phases of the cell cycle (PubMed:19843527). Cytoplasmic during mitosis, after breakup of the nuclear membrane (PubMed:19843527) Localizes to replication forks (PubMed:33412112) |
Tissue Location | Overexpressed in prostate adenocarcinomas and high- grade prostatic intraepithelial neoplasia |
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Background
Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed.
References
Wada K, et al. Biochim Biophys Acta. 2002. 1591:1.
Cimato TR, et al. J Neurosci Res. 2002. 67:435.
Frankel A, et al. J Biol Chem. 2002. 277:3537.
Brahms H, et al. RNA. 2001. 7:1531.
Pelletier M, et al. Mol Biochem Parasitol. 2001. 118:49.
Belyanskaya LL, et al. J Biol Chem. 2001. 276:18681.
Rho J, et al. J Biol Chem. 2001. 276:11393.
Scorilas A, et al. Biochem Biophys Res Commun. 2000. 278:349.
Frankel A, et al. J Biol Chem. 2000. 275:32974.
Zhang X, et al. EMBO J. 19:3509.
Tang J, et al. J Biol Chem. 1998. 273:16935.
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