Phospho-ATF-2 (Thr69/71)/ATF-7 (Thr51/53) (E6A8A) Rabbit mAb (BSA and Azide Free) #94125
- WB
- IF
- F
Supporting Data
REACTIVITY | H M R |
SENSITIVITY | Endogenous |
MW (kDa) | 65, 75 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
Phospho-ATF-2 (Thr69/71)/ATF-7 (Thr51/53) (E6A8A) Rabbit mAb (BSA and Azide Free) detects endogenous levels of ATF-2 only when dually phosphorylated at both Thr69 and Thr71, and ATF-7 only when dually phosphorylated at both Thr51 and Thr53. It does not recognize ATF-2 singly phosphorylated at either Thr69 or Thr71, and it does not recognize ATF-7 singly phosphorylated at either Thr51 or Thr53.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr69 and 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.
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