Description
Product Usage Information
Western Blotting: 1:1000
Immunoprecipitation: 1:100
Immunohistochemistry (Paraffin): 1:200 - 1:800
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody.
Protocol
Available protocols: Western Blotting, Immunoprecipitation, Immunohistochemistry (Paraffin)
Specificity / Sensitivity
4E-BP2 Antibody detects endogenous levels of total 4E-BP2, independent of phosphorylation. This antibody does not cross-react significantly with 4E-BP1.
Species Reactivity: Human, Mouse, Rat, Monkey, Bovine
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxy-terminus of human 4E-BP2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Translation repressor protein 4E-BP1 (also known as PHAS-1) inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation (1). Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity (2,3). Multiple 4E-BP1 residues are phosphorylated (4). While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70 (5). 4E-BP2 and 4E-BP3 share high sequence homology with 4E-BP1, including conservation of the major FRAP/mTOR-dependent phosphorylation sites. Preliminary data suggests that phosphorylation of 4E-BP2 is regulated in a similar manner to that of 4E-BP1, although phosphorylation of this protein has not been as extensively studied (6).
Alternate Names
4E-BP2; 4EBP2; eIF4E-binding protein 2; EIF4EBP2; eukaryotic translation initiation factor 4E binding protein 2; Eukaryotic translation initiation factor 4E-binding protein 2; PHASII; phosphorylated, heat and acid stable regulated by insulin protein II
