PRMT6 Antibody [K2N19] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:30 IF1:50 FCM1:50

Application
WB, IP, IF, FCM

Reactivity
Human

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 Observed MW
42 kDa 42 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
PRMT6 Antibody [K2N19] detects endogenous levels of total PRMT6 protein.

Clone
K2N19

Synonym(s)
HRMT1L6, PRMT6, Protein arginine N-methyltransferase 6, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6, Histone-arginine N-methyltransferase PRMT6

Background
PRMT6 is a type I protein arginine methyltransferase of the PRMT family that localizes predominantly to the nucleus, where it transfers methyl groups from S‑adenosylmethionine to arginine residues on histones and nonhistone proteins to control chromatin structure, gene expression, and signaling outputs in proliferating cells and diverse tumor types. The enzyme contains the canonical PRMT catalytic core with a Rossmann‑like fold and conserved THW and double‑E motifs that position the arginine substrate and cofactor, and this architecture supports asymmetric dimethylation of arginine side chains on histone H3 as well as multiple regulatory proteins. PRMT6 deposits a repressive H3R2me2a mark at promoters and enhancers, which antagonizes H3K4 methylation and reduces transcriptional activation of select tumor suppressor and cell‑cycle inhibitor genes, aligning its chromatin activity with maintenance of a proliferative transcriptional program. PRMT6 also methylates several signaling and cell‑cycle regulators, including the CDK inhibitor p21 and the lipid phosphatase PTEN, and these modifications alter their localization, stability, and pathway coupling. Arginine methylation of p21 at a defined C‑terminal site promotes phosphorylation on a neighboring threonine residue, increases retention of p21 in the cytoplasm, and is associated with stronger CDK2–cyclin E activity and reduced nuclear CDK inhibition, thereby favoring DNA synthesis and resistance to cytotoxic agents. Arginine methylation of PTEN on specific residues by PRMT6 decreases PI3K–AKT pathway activity and also influences pre‑mRNA splicing patterns through effects on PTEN function in the nucleus, adding a layer by which PRMT6 connects methylation of a tumor suppressor to modulation of both survival signaling and RNA processing.

Background

PRMT6 is a type I protein arginine methyltransferase of the PRMT family that localizes predominantly to the nucleus, where it transfers methyl groups from S‑adenosylmethionine to arginine residues on histones and nonhistone proteins to control chromatin structure, gene expression, and signaling outputs in proliferating cells and diverse tumor types. The enzyme contains the canonical PRMT catalytic core with a Rossmann‑like fold and conserved THW and double‑E motifs that position the arginine substrate and cofactor, and this architecture supports asymmetric dimethylation of arginine side chains on histone H3 as well as multiple regulatory proteins. PRMT6 deposits a repressive H3R2me2a mark at promoters and enhancers, which antagonizes H3K4 methylation and reduces transcriptional activation of select tumor suppressor and cell‑cycle inhibitor genes, aligning its chromatin activity with maintenance of a proliferative transcriptional program. PRMT6 also methylates several signaling and cell‑cycle regulators, including the CDK inhibitor p21 and the lipid phosphatase PTEN, and these modifications alter their localization, stability, and pathway coupling. Arginine methylation of p21 at a defined C‑terminal site promotes phosphorylation on a neighboring threonine residue, increases retention of p21 in the cytoplasm, and is associated with stronger CDK2–cyclin E activity and reduced nuclear CDK inhibition, thereby favoring DNA synthesis and resistance to cytotoxic agents. Arginine methylation of PTEN on specific residues by PRMT6 decreases PI3K–AKT pathway activity and also influences pre‑mRNA splicing patterns through effects on PTEN function in the nucleus, adding a layer by which PRMT6 connects methylation of a tumor suppressor to modulation of both survival signaling and RNA processing.

References
https://pubmed.ncbi.nlm.nih.gov/30886105/ https://pubmed.ncbi.nlm.nih.gov/35311114/

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%