Technical Data
4E Binding Protein 1 (Protein Synthesis Initiation Factor 4E Binding Protein, eIF-4EBP1, PHAS-1, PHAS-I, Eukaryotic Translation Initiation Factor BP)
4E-BP1 (eIF4E-binding protein) also known as PHAS, is a 10-12kD 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. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)

Suitable for use in Flow Cytometry, Western Blotting, Immunoprecipitation, Immunohistochemistry, Immunocytochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:5000-10000
Immunohistochemistry: 1:100-250
Immunocytochemistry: 1:100-250
Flow Cytometry: 1:20
Immunoprecipitation: 1:50

Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
100ul-20°CBlue IceHumanRabbit
A synthetic peptide corresponding to residues near the N-term of human4E-BP1.
Supplied as a liquid
Recognizes human 4E-BP1.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Pause, A., G.J. Belsham, A.-C. Gingras, O. Donzé, T.A. Lin, J.C. Lawrence, Jr., and N. Sonenberg. 1994. Nature 371: 762-767 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, 13180–13185 4. Trumpp, A., Refaeli, Y., Oskarsson, T., Gasser, S., Murphy, M., Martin, G. R., and Bishop, J. M. (2001) Nature 414, 768–773