PRMT4/CARM1 Antibody [J8A9] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Usage Information

Dilution
WB1:1000 IP1:50 IF1:200 - 1:400

Application
WB, IP, IF

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
63 kDa

Positive Control	HeLa cells; NIH/3T3 cells; H-4-II-E cells; COS-7 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
PRMT4/CARM1 Antibody [J8A9] detects endogenous levels of total PRMT4/CARM1 protein.

Clone
J8A9

Synonym(s)
Histone-arginine methyltransferase CARM1; Coactivator-associated arginine methyltransferase 1; Protein arginine N-methyltransferase 4; CARM1; PRMT4

Background
PRMT4, also known as CARM1 (coactivator-associated arginine methyltransferase 1), is a Type I protein arginine methyltransferase that catalyzes the asymmetric dimethylation of arginine residues using S-adenosylmethionine (SAM) as a methyl donor, uniquely targeting proline-, glycine-, and methionine-rich (PGM) motifs instead of the glycine-arginine-rich domains favored by other PRMTs. CARM1 consists of an N-terminal domain with a PHD-like zinc knuckle homology region that mediates protein interactions, a central catalytic core of about 340 residues containing conserved PRMT motifs (including IxxW, DxxY, SExxMGLG, THW, QxWxYDPFxR, and DxxPxWxxFxxH), and essential residues such as Glu258 and Asp305 that, along with the SAM-binding pocket, enable the methylation reaction on substrate arginine guanidinium groups. This catalytic region is flanked by a C-terminal transactivation domain that facilitates coactivator recruitment. CARM1’s primary function is the methylation of histone H3 at arginine residues 17 and 26, which promotes transcriptional activation by nuclear receptors such as ERα, RAR, and AR in cooperation with coactivators like p300/CBP, thereby enhancing chromatin accessibility and gene expression during differentiation. CARM1 modifies non-histone substrates including SRC-3, HuR, and CBP, impacting mRNA splicing, stability, export via paraspeckles, autophagy, metabolism, and signal transduction. Biologically, CARM1 is critical for retinoic acid-induced embryonic stem cell differentiation into extraembryonic endoderm by repressing pluripotency genes like Rex1 and activating RA-responsive targets such as CRABP2 and NR2F1. It also influences pre-mRNA processing through H3R17 methylation near splice sites and localizes to nuclear speckles and paraspeckles, where it regulates RNA metabolism. Overexpression of CARM1 is linked to poor prognosis in breast cancer, prostate cancer, and myeloma, promoting oncogenesis through enhanced steroid signaling and increased proliferation. CARM1 activity is modulated by post-translational modifications such as phosphorylation, O-GlcNAcylation, and ubiquitination, and selective inhibitors have demonstrated antitumor efficacy in vivo.

Background

PRMT4, also known as CARM1 (coactivator-associated arginine methyltransferase 1), is a Type I protein arginine methyltransferase that catalyzes the asymmetric dimethylation of arginine residues using S-adenosylmethionine (SAM) as a methyl donor, uniquely targeting proline-, glycine-, and methionine-rich (PGM) motifs instead of the glycine-arginine-rich domains favored by other PRMTs. CARM1 consists of an N-terminal domain with a PHD-like zinc knuckle homology region that mediates protein interactions, a central catalytic core of about 340 residues containing conserved PRMT motifs (including IxxW, DxxY, SExxMGLG, THW, QxWxYDPFxR, and DxxPxWxxFxxH), and essential residues such as Glu258 and Asp305 that, along with the SAM-binding pocket, enable the methylation reaction on substrate arginine guanidinium groups. This catalytic region is flanked by a C-terminal transactivation domain that facilitates coactivator recruitment. CARM1’s primary function is the methylation of histone H3 at arginine residues 17 and 26, which promotes transcriptional activation by nuclear receptors such as ERα, RAR, and AR in cooperation with coactivators like p300/CBP, thereby enhancing chromatin accessibility and gene expression during differentiation. CARM1 modifies non-histone substrates including SRC-3, HuR, and CBP, impacting mRNA splicing, stability, export via paraspeckles, autophagy, metabolism, and signal transduction. Biologically, CARM1 is critical for retinoic acid-induced embryonic stem cell differentiation into extraembryonic endoderm by repressing pluripotency genes like Rex1 and activating RA-responsive targets such as CRABP2 and NR2F1. It also influences pre-mRNA processing through H3R17 methylation near splice sites and localizes to nuclear speckles and paraspeckles, where it regulates RNA metabolism. Overexpression of CARM1 is linked to poor prognosis in breast cancer, prostate cancer, and myeloma, promoting oncogenesis through enhanced steroid signaling and increased proliferation. CARM1 activity is modulated by post-translational modifications such as phosphorylation, O-GlcNAcylation, and ubiquitination, and selective inhibitors have demonstrated antitumor efficacy in vivo.

References
https://pubmed.ncbi.nlm.nih.gov/30153436/ https://pubmed.ncbi.nlm.nih.gov/33485722/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%