Datasheet

生物学的記述

Specificity	PRMT2 Antibody [G16H19] detects endogenous levels of total PRMT2 protein.
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.

Specificity

PRMT2 Antibody [G16H19] detects endogenous levels of total PRMT2 protein.

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.

使用情報

Application

WB, IHC, IF, ELISA

Dilution

WB	IHC	IF
1:1000-1:6000	1:500-1:2000	1:200-1:800

Reactivity

Human, Mouse, Rat

Source

Mouse Monoclonal Antibody

MW

49 kDa

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

プロトコール

References

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

Application Data

WB

Validated by Selleck

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