Product Pathways - DNA Damage
Phospho-ATR (Ser428) Antibody #2853
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W | H M R Mk | 300 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Phospho-ATR (Ser428) Antibody detects endogenous levels of ATR only when phosphorylated at serine 428.
Source / Purification
Polyclonal antibodies are prepared by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Ser428 of human ATR. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of Raw264.7, SV-T2 and HT-29 cells that were untreated or UV-treated (50 mJ, 30 min), using Phospho-ATR (Ser428) Antibody. Lambda phosphatase NEB #P0753 (10,000 Units/ml, 1hr) was used to demonstrate the phospho-specificity of the antibody.
Western Blotting
Western blot analysis of untreated, UV-treated (50 mJ, 30 min) and nocodazole-treated (50 ng/ml, 24hr) Raw264.7 cells, using Phospho-ATR (Ser428) Antibody (upper) and a total ATR antibody (lower).
Background
Ataxia telangiectasia mutated kinase (ATM) and ataxia telangiectasia and Rad3-related kinase (ATR) are PI-3 Kinase-related kinase (PIKK) family members that phosphorylate multiple substrates on serine or threonine residues that are followed by a glutamine in response to DNA damage or replication blocks (1-3). Despite the essential role of ATR in cell cycle signaling and DNA repair processes, little is known about its activation. While there have been no published reports of phosphorylation sites on ATR, Cell Signaling Technology has produced an antibody directed against phospho-ATR (Ser428) that demonstrates in vivo and UV-induced phosphorylation of this protein. This reagent could prove to be a valuable tool for monitoring ATR activation. Proline-directed phosphorylation sites like this one are often targeted by CDKs and MAPKs and can often dramatically affect protein conformation (4,5).
- Kastan, M.B. and Lim, D.S. (2000) Nat. Rev. Mol. Cell Biol. 1, 179-186.
- Abraham, R.T. (2004) DNA Repair (Amst) 3, 883-887.
- Shechter, D. et al. (2004) DNA Repair (Amst) 3, 901-908.
- Pinna, L.A. and Ruzzene, M. (1996) Biochim. Biophys. Acta 1314, 191-225.
- Zhou, X.Z. et al. (1999) Cell Mol. Life Sci. 56, 788-806.
Application References
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