4E-BP1 (EIF4EBP1) antibody RabMAb®

Cat.#: 1578-1
Abcam ID: ab32130

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 not (2). 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. However, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)

Recommended Applications

WB, IHC, IP, FC

Applications and Recommended Dilution Factors

WB: 1:1,000 - 10,000
IHC: 1:50-100
IP: 1:50
FC: 1:20

Species Reactivity *

Human

*Cross reactivity determined by western blot only.

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Products Data

A. Western blot analysis on K562 cell lysate using anti-4E-BP1 RabMAb (cat. # 1578-1), dilution 1:1,000.	B. Immunohistochemical analysis of paraffin-embedded human prostate carcinoma using anti-4E-BP1 RabMAb (cat. # 1578-1).

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Specificity

A synthetic peptide corresponding to residues near the C-term of human4E-BP1 was used as immunogen.

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., G.J. Belsham, A.-C. Gingras, O. Donz
2. Gingras, A.-C., S.G. Kennedy, M.A. O'Leary, N. Sonenberg, and N. Hay. 1998. Genes & Dev. 12: 502-513
3. Iritani, B. M., and Eisenman, R. N. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13180
4. Trumpp, A., Refaeli, Y., Oskarsson, T., Gasser, S., Murphy, M., Martin, G. R., and Bishop, J. M. (2001) Nature 414, 768

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