Technical Data
4E Binding Protein 1,2,3, phosphorylated (pT45) (4EBP1, 4E-BP1, 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 10-12 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)

Suitable for use in Western Blot, Immunoprecipitation, Immunohistochemistry and Immunocytochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:5000
Immunoprecipitation: 1:10
Immunohistochemistry: 1:50
Immunocytochemistry: 1:100
Optimal dilution determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. 

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
100ul-20°CBlue IceHumanRabbit
Not Determined
Phospho specific peptide corresponding to residues surrounding threonine 45 of human 4E Binding Protein 1,2,3.
Supplied as a liquid in 50mM Tris-Glycine, pH 7.4, 0.15M sodium chloride, 0.05% BSA, 0.01% sodium azide, 40% glycerol.
Recognizes human 4E Binding Protein 1,2,3 at ~15-20kD when phosphorylated at threonine 45. Species Crossreactivity: mouse
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
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, 13180–13185. 4. Trumpp, A. et al. Nature 414, 768.