4E-BP2 Antibody #2845
Filter:
- WB
- IP
- IHC
Supporting Data
| REACTIVITY | H M R Mk B |
| SENSITIVITY | Endogenous |
| MW (kDa) | 15 to 20 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
- B-Bovine
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| 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
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 in vivo (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).
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).
- Pause, A. et al. (1994) Nature 371, 762-7.
- Brunn, G.J. et al. (1997) Science 277, 99-101.
- Gingras, A.C. et al. (1998) Genes Dev 12, 502-13.
- Fadden, P. et al. (1997) J Biol Chem 272, 10240-7.
- Gingras, A.C. et al. (1999) Genes Dev 13, 1422-37.
- Lin, T.A. and Lawrence, Jr, J.C. (1996) J. Biol. Chem. 271, 30199-30204.
限制使用
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