Phospho-ATF-2 (Thr71)/ATF-7 (Thr53) (A8J7P) Rabbit mAb #15411
- WB
- F
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 65,75 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Flow Cytometry (Fixed/Permeabilized) | 1:1600 |
Storage
For a carrier free (BSA and azide free) version of this product see product #46615.
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr71 of human ATF-2 protein.
Background
The transcription factor ATF-2 (also called CRE-BP1) binds to both AP-1 and CRE DNA response elements and is a member of the ATF/CREB family of leucine zipper proteins (1). ATF-2 interacts with a variety of viral oncoproteins and cellular tumor suppressors and is a target of the SAPK/JNK and p38 MAP kinase signaling pathways (2-4). Various forms of cellular stress, including genotoxic agents, inflammatory cytokines, and UV irradiation, stimulate the transcriptional activity of ATF-2. Cellular stress activates ATF-2 by phosphorylation of Thr69 and Thr71 (2-4). Both SAPK and p38 MAPK have been shown to phosphorylate ATF-2 at these sites in vitro and in cells transfected with ATF-2. Mutations of these sites result in the loss of stress-induced transcription by ATF-2 (2-4). In addition, mutations at these sites reduce the ability of E1A and Rb to stimulate gene expression via ATF-2 (2).
ATF-7 is another member of the ATF/CREB family of leucine zipper proteins (5). Similarly, Thr51 and Thr53 (corresponding to Thr69 and Thr71 of ATF-2, respectively) can be phosphorylated under different conditions (6,7).
- Abdel-Hafiz, H.A. et al. (1992) Mol Endocrinol 6, 2079-89.
- Gupta, S. et al. (1995) Science 267, 389-93.
- van Dam, H. et al. (1995) EMBO J 14, 1798-811.
- Livingstone, C. et al. (1995) EMBO J 14, 1785-97.
- Peters, C.S. et al. (2001) J Biol Chem 276, 13718-26.
- Camuzeaux, B. et al. (2008) J Mol Biol 384, 980-91.
- Maekawa, T. et al. (2010) EMBO J 29, 196-208.
Limited Uses
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