PRMT2 Antibody [G16H19] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Lane 1: Hela, Lane 2: LNCaP, Lane 3: Jurkat, Lane 4: SK-OV-3

Usage Information

Dilution
WB1:1000-1:6000 IHC1:500-1:2000 IF1:200-1:800

Application
WB, IHC, IF, ELISA

Reactivity
Human, Mouse, Rat

Source
Mouse 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
49 kDa 45-50 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
PRMT2 Antibody [G16H19] detects endogenous levels of total PRMT2 protein.

Clone
G16H19

Synonym(s)
Protein arginine N-methyltransferase 2; Histone-arginine N-methyltransferase PRMT2; PRMT2; HMT1; HRMT1L1

Background
PRMT2 belongs to the protein arginine methyltransferase family as a type I enzyme that predominantly generates asymmetric dimethylarginine modifications on target substrates. It features a catalytic core with an S-adenosylmethionine binding domain flanked by regulatory regions that facilitate substrate recognition and protein-protein interactions. PRMT2 methylates histone H3 at arginine R8 to deposit H3R8me2a marks at promoters of oncogenic genes, recruiting transcriptional machinery to activate cell cycle regulators, proliferation factors, and invasion-associated transcripts in glioblastoma cells. This histone modification integrates with hypoxia-responsive pathways, enhancing tumor cell migration and chemoresistance under low oxygen conditions while sustaining glycolytic metabolism. PRMT2 forms complexes with the retinoblastoma protein RB and E2F1, symmetrically dimethylating RB to repress E2F1-driven G1/S transition and modulate cell cycle entry. Interaction with splicing factors like SAM68 via its SH3 domain alters alternative splicing patterns, influencing RNA processing of genes involved in signal transduction and stress responses. PRMT2 also methylates non-histone substrates to fine-tune NF-κB signaling by retaining nuclear IκBα, which blocks NF-κB nuclear export and attenuates inflammatory cytokine production. PRMT2 supports transcriptional coactivation in differentiating cells and RNA transport during development. Elevated nuclear PRMT2 expression correlates with high-grade gliomas and poor patient outcomes, while its depletion impairs tumorigenesis and sensitizes cells to therapy.

Background

PRMT2 belongs to the protein arginine methyltransferase family as a type I enzyme that predominantly generates asymmetric dimethylarginine modifications on target substrates. It features a catalytic core with an S-adenosylmethionine binding domain flanked by regulatory regions that facilitate substrate recognition and protein-protein interactions. PRMT2 methylates histone H3 at arginine R8 to deposit H3R8me2a marks at promoters of oncogenic genes, recruiting transcriptional machinery to activate cell cycle regulators, proliferation factors, and invasion-associated transcripts in glioblastoma cells. This histone modification integrates with hypoxia-responsive pathways, enhancing tumor cell migration and chemoresistance under low oxygen conditions while sustaining glycolytic metabolism. PRMT2 forms complexes with the retinoblastoma protein RB and E2F1, symmetrically dimethylating RB to repress E2F1-driven G1/S transition and modulate cell cycle entry. Interaction with splicing factors like SAM68 via its SH3 domain alters alternative splicing patterns, influencing RNA processing of genes involved in signal transduction and stress responses. PRMT2 also methylates non-histone substrates to fine-tune NF-κB signaling by retaining nuclear IκBα, which blocks NF-κB nuclear export and attenuates inflammatory cytokine production. PRMT2 supports transcriptional coactivation in differentiating cells and RNA transport during development. Elevated nuclear PRMT2 expression correlates with high-grade gliomas and poor patient outcomes, while its depletion impairs tumorigenesis and sensitizes cells to therapy.

References
https://pubmed.ncbi.nlm.nih.gov/34833139/ https://pubmed.ncbi.nlm.nih.gov/30382083/

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%