Phospho-Noxa (Ser13) (E8I9P) Rabbit mAb #41967
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Transfected Only |
| MW (kDa) | 10 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Noxa (Ser13) (E8I9P) Rabbit mAb recognizes transfected levels of Noxa protein only when phosphorylated at Ser13. A band of unknown identity is detected at 28 kDa.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser13 of human Noxa protein.
Background
Phorbol-12-myristate-13-acetate-induced protein 1 (PMAIP1, Noxa) is a small protein that plays a key role in mediating apoptotic signaling. Noxa is a pro-apoptotic Bcl-2 family protein that contains a single Bcl-2 homology (BH3) domain (1). Members of the “BH3-only” family (e.g., Noxa, Bad, Bim, Puma, Bid, Bik, and Hrk) are highly regulated proteins that induce apoptosis through BH3-dependent interaction with anti-apoptotic Bcl-2 family proteins (2). Noxa localizes to mitochondria and binds the anti-apoptotic proteins Mcl-1 and A1/Bfl-1, but does not bind to Bcl-2 or Bcl-xL (3). The Noxa protein competes with Mcl-1 for binding to mitochondrial Bak protein. Noxa was originally identified as a phorbol ester inducible protein that is highly expressed in adult T-cell leukemia cell lines (4). Several different stimuli, including DNA damage, hypoxia, interferon, viral infection, and double-stranded RNA, induce Noxa expression in cells. Higher levels of Noxa protein are typically found in hematopoietic cells (3,5,6).
Phosphorylation of Noxa at Ser13 by CDK5 was found to inhibit its apoptotic activity (7).
- Ploner, C. et al. (2008) Oncogene 27 Suppl 1, S84-92.
- Bouillet, P. and Strasser, A. (2002) J Cell Sci 115, 1567-74.
- Oda, E. et al. (2000) Science 288, 1053-8.
- Hijikata, M. et al. (1990) J Virol 64, 4632-9.
- Kim, J.Y. et al. (2004) J Exp Med 199, 113-24.
- Sun, Y. and Leaman, D.W. (2005) J Biol Chem 280, 15561-8.
- Lowman, X.H. et al. (2010) Mol Cell 40, 823-33.
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