供货周期: | 一周 |
品牌: | |
规格: | 100ul |
货号: | 2250-1 |
CAS号: |
4E-BP1 Phospho(pT70)(EIF4EBP1)antibody
Cat.#: 2250-1
Rabbit Monoclonal Antibody
Clone ID: EPR654(2)A
Swiss Prot: Q13541
Mol Weight: 17kDa
Size: 100ul
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 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, 70 or serine 64. Although, not all phosphorylation events equally block the 4EBP1-eIF4E interaction (3-4)
Recommended Applications
WB, IHC
Applications and Recommended Dilution Factors
WB: 1:1,000 - 10,000
IHC: 1:100
Species Reactivity
Human
Cross reactivity determined by western blot only.
Products Data
A. Western blot analysis on 293T cell lysates using anti-Phospho-4E-BP1 (pT70) RabMAb (cat. #2250-1), 1:500 dilution. Cells were either (A) untreated (B) treated with FBS.
Specificity
A phospho specific peptide corresponding to residues surrounding threonine 70 was used as an immunogen. This antibody detects 4E-BP1 phosophorylated at threonine 70.
Storage Condition and Buffer
Store at -20 °C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Alternative Names
EIF4EBP1 antibody, 4E-BP1 antibody, 4EBP1 antibody, BP-1 antibody, MGC4316 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., 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
4. Trumpp, A. et al. Nature 414, 768
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