Upstream / Downstream


Explore pathways related to this product.

Our U.S. Offices Are Closed

Our U.S. offices are closed in observance of Memorial Day. We will reopen on Tuesday, May 30th.

Thank you for your patience.


Find answers on our FAQs page.


PhosphoSitePlus® Resource

  • Additional protein information
  • Analytical tools


MW (kDa)

Figure 1. Western blot analysis of ATF-2 fusion protein phosphorylated by different isoforms of p38 kinase, using ATF-2 (20F1) Rabbit mAb #9226 (upper panel) and Phospho-ATF-2 (Thr71) (11G2) Rabbit mAb #5112 (lower panel).

Learn more about how we get our images

Figure 2. ATF-2 fusion protein was used as substrate to measure p38 kinases activity in a radiometric assay using the following reaction conditions: 25 mM Tris-HCl (pH7.5), 10 mM MgCl2, 5 mM b-glycerophosphate, 0.1 mM Na3VO4, 2 mM DTT, 50 μM ATP, Substrate: ATF-2 fusion protein 400 ng/μL, and p38 kinases: 100 ng/25 μL.

Learn more about how we get our images

Product Description

Activating Transcription Factor 2 (ATF-2) Fusion Protein serves as a useful substrate for SAPK/JNK and p38 MAP kinases. It is expressed as a recombinant protein fusion containing ATF-2 residues 19-96. It contains the amino-terminal activation domain of ATF-2, which is regulated by phosphorylation of Thr69 and Thr71.

Molecular Formula:

Molecular Weight: 34 kDa

Product Usage Information

ATF-2 Fusion Protein, at a concentration of 2 µg/20 µl reaction, can be phosphorylated by an upstream kinase in an in vitro kinase assay with 1X Kinase Buffer (#9802) and 200 µM ATP (#9804). After a 30-minute assay at 30ºC, phosphorylation can be detected by Western blot with Phospho-ATF-2 (Thr71) Antibody (#9221).

Storage: Store at -20°C.

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).

1.  Abdel-Hafiz, H.A. et al. (1992) Mol Endocrinol 6, 2079-89.

2.  Gupta, S. et al. (1995) Science 267, 389-93.

3.  van Dam, H. et al. (1995) EMBO J 14, 1798-811.

4.  Livingstone, C. et al. (1995) EMBO J 14, 1785-97.

Entrez-Gene Id 1386
Swiss-Prot Acc. P15336

For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

ATF-2 Fusion Protein