PRMT2 Antibody [G16H19]

Catalog No.: F5119

Application: Reactivity: Human, Mouse, Rat

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

当該製品は品切れ状态で、ごメールアドレスを教えていただければ、在庫があると、メールで顧客様に伝えます。

代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

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

Application
WB, IHC, IF, ELISA

Source
Mouse Monoclonal Antibody

Reactivity
Human, Mouse, Rat

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
^*なぜ予測分子量と実際の分子量が異なるのか？下記の原因により、実際の分子量が予測と異なる：タンパク質の翻訳後修飾（リン酸化/糖鎖付加），スプライシングバリアント，イソフォーム，相対的な電荷，ポリマー。

Datasheet & SDS

生物学的記述

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
[1] Cura V, et al. Life (Basel). 2021 Nov 19;11(11):1263. [2] Dong F, et al. Nat Commun. 2018 Oct 31;9(1):4552.

PVDFメンブレン孔径参考表

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

技術サポート

ストックの作り方、阻害剤の保管方法、細胞実験や動物実験の際に注意すべき点など、製品を取扱う時に問い合わせが多かった質問に対しては取扱説明書でお答えしています。

Handling Instructions

他に質問がある場合は、お気軽にお問い合わせください。

* 必須

* 大学・企業名 大学・企業名を記入してください

* 名前 名前を記入してください

* 電子メール 電子メール・アドレスを記入してください 有効なメールアドレスを入力してください

電話番号

* 内容 お問い合わせ内容をご入力ください

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%