Phospho-eIF4E (Ser209) Antibody [G23F17]

Catalog No.: F5399

Application: Reactivity: Human, Mouse, Rat

Lane 1: 293T, Lane 2: 293T (Anisomycin, 25 μg/mL, 30 min), Lane 3: Hela, Lane 4: Hela (Anisomycin, 25 μg/mL, 30 min)

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

使用情報

Dilution
WB1:1000 IP1:200

Application
WB, IP

Source
Rabbit 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
25 kDa

Datasheet & SDS

生物学的記述

Specificity
Phospho-eIF4E (Ser209) Antibody [G23F17] detects endogenous levels of total eIF4E protein only when it is phosphorylated at Ser209.

Clone
G23F17

Synonym(s)
Eukaryotic translation initiation factor 4E; eIF-4E; EIF4E

Background
Phospho‑eIF4E (Ser209) marks a key regulatory site on the mRNA 5′ cap‑binding initiation factor 4E (eIF4E), a central node in the control of cap‑dependent translation that functions within the eIF4F complex alongside the scaffold eIF4G and the RNA helicase eIF4A. eIF4E recognizes the 7‑methylguanosine cap of 5′‑capped mRNAs, and its interaction with eIF4G stabilizes the eIF4F complex and facilitates ribosome recruitment, while post‑translational modification at Ser209 by the MAPK‑activated kinases Mnk1 and Mnk2 fine‑tunes both the affinity and functional output of eIF4E without disrupting eIF4E–eIF4G binding per se. Activation of ERK and p38 MAPK cascades mobilizes Mnk1/2 to phosphorylate eIF4E at Ser209 within the C‑terminal domain, an event that enhances the translation of a subset of mRNAs encoding growth‑ and survival‑related proteins such as cyclins and anti‑apoptotic factors, thereby coupling extracellular cues to selective production of malignancy‑associated proteins. Ser209 phosphorylation increases resistance to oxidative, nutrient, and cytotoxic stresses by promoting recovery‑phase protein synthesis and upregulating pro‑survival factors such as Mcl‑1, and in tumorigenesis persistent eIF4E Ser209 phosphorylation drives proliferation, metastasis, and therapeutic resistance, whereas blocking Mnk‑dependent eIF4E phosphorylation suppresses eIF4E‑driven oncogenic translation and tumor growth.

Background

Phospho‑eIF4E (Ser209) marks a key regulatory site on the mRNA 5′ cap‑binding initiation factor 4E (eIF4E), a central node in the control of cap‑dependent translation that functions within the eIF4F complex alongside the scaffold eIF4G and the RNA helicase eIF4A. eIF4E recognizes the 7‑methylguanosine cap of 5′‑capped mRNAs, and its interaction with eIF4G stabilizes the eIF4F complex and facilitates ribosome recruitment, while post‑translational modification at Ser209 by the MAPK‑activated kinases Mnk1 and Mnk2 fine‑tunes both the affinity and functional output of eIF4E without disrupting eIF4E–eIF4G binding per se. Activation of ERK and p38 MAPK cascades mobilizes Mnk1/2 to phosphorylate eIF4E at Ser209 within the C‑terminal domain, an event that enhances the translation of a subset of mRNAs encoding growth‑ and survival‑related proteins such as cyclins and anti‑apoptotic factors, thereby coupling extracellular cues to selective production of malignancy‑associated proteins. Ser209 phosphorylation increases resistance to oxidative, nutrient, and cytotoxic stresses by promoting recovery‑phase protein synthesis and upregulating pro‑survival factors such as Mcl‑1, and in tumorigenesis persistent eIF4E Ser209 phosphorylation drives proliferation, metastasis, and therapeutic resistance, whereas blocking Mnk‑dependent eIF4E phosphorylation suppresses eIF4E‑driven oncogenic translation and tumor growth.

References
[1] Furic L, et al. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14134-9. [2] Martínez A, et al. PLoS One. 2015 Apr 29;10(4):e0123352.

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

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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%