4E-BP1/2/3 Phospho (pT45) (EIF4EBP1) antibody RabMAb®

Cat.#: 2334-1
Abcam ID: ab68187

Rabbit Monoclonal Antibody

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Bulk and Custom formulation available Email request

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Description

4E-BP1 (eIF4E-binding protein) also known as PHAS, is a 10-12 kDa acidic protein that compete with eIF4G for binding of eiF4E to the mRNA 5 cap structure (1). Binding of the 4E-BPs to eIF4E is reversible and is dependent on the phosphorylation status of 4E-BP. Non-phosphorylated 4E-BP1 will bind strongly to eiF4E while, the phosphorylated form will no (2)t. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating 4E-BP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 64. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)

Recommended Applications

WB, IHC, ICC, IP

Applications and Recommended Dilution Factors

WB: 1:1,000 - 5,000
IHC: 1:50
ICC: 1:100
IP: 1:10

Species Reactivity *

Human, Mouse

*Cross reactivity determined by western blot only.

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Products Data

A. Western blot analysis on 293T cell lysates using anti-Phospho-4E-Bp1/2/3 (pT45) RabMAb (cat. #2334-1). Cells were either (A) untreated (B) treated with FBS.	B. Immunohistochemical analysis of paraffin-embedded human breast carcinoma using anti-4E-BPE1 RabMAb (cat. # 2334-1).

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Specificity

A phospho specific peptide corresponding to residues surrounding threonine 45 was used as an immunogen. This antibody detects 4E-BP1/2/3 phosphorylated at threonine 45.

Storage Condition and Buffer

Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.

Alternative Names

EIF4EBP1 antibody, 4E-BP1 antibody, 4EBP1 antibody, BP-1 antibody, PHAS-I antibody, Eukaryotic translation initiation factor 4E-binding protein 1 antibody, Phosphorylated heat- and acid-stable protein regulated by insulin 1 antibody

Description References

1. Pause, A., et al. 1994. Nature 371: 762-767
2. Gingras, A.-C., et al. Genes & Dev. 12: 502-513, 1998
3. Iritani, BM et al. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13180
4. Trumpp, A. et al. Nature 414, 768

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