Cell Signaling Technology

Product Pathways - DNA Damage

ATR Antibody #2790

Applications Reactivity MW (kDa) Source
W IP IF-IC H M R Mk Hm (B) (Dg) 250 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Hm=Hamster  B=Bovine  Dg=Dog
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

ATR Antibody detects endogenous levels of total ATR protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to central residues of human ATR. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using ATR Antibody.

IP

IP

Immunoprecipitation of ATR from HeLa cell lysates using ATR Antibody. Western blot detection was performed using the same antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of HeLa cells using ATR Antibody (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red).


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).

  1. Kastan, M.B. and Lim, D.S. (2000) Nat. Rev. Mol. Cell Biol. 1, 179-186.
  2. Abraham, R.T. (2004) DNA Repair (Amst) 3, 883-887.
  3. Shechter, D. et al. (2004) DNA Repair (Amst) 3, 901-908.
  4. Pinna, L.A. and Ruzzene, M. (1996) Biochim. Biophys. Acta 1314, 191-225.
  5. Zhou, X.Z. et al. (1999) Cell Mol. Life Sci. 56, 788-806.

Application References

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