Cell Signaling Technology

Product Pathways - DNA Damage

Phospho-ATRIP (Ser224) Antibody #5161

Applications Reactivity Sensitivity MW (kDa) Source
W H (M) (Mk) Endogenous 86 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-ATRIP (Ser224) Antibody detects endogenous levels of ATRIP protein only when phosphorylated at Ser224.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phoshopeptide corresponding to residues surrounding Ser224 of the human ATRIP protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, untreated or treated with λ and calf intestinal phosphatases, using Phospho-ATRIP (Ser224) Antibody (upper) or ATRIP Antibody #2737 (lower).

Background

In response to genomic stress, the ATR interacting protein (ATRIP) binds and is phosphorylated by the DNA damage-and checkpoint-activated kinase ATR (ataxia-telangiectasia mutated and rad3-related). Both ATR and ATRIP are integral for checkpoint signaling and are critical in the DNA repair response (1-3). Direct interaction between ATRIP and replication protein A (RPA) at RPA-coated, single-stranded DNA results in the recruitment of phosphorylated ATR/ATRIP to stalled replication forks and sites of DNA damage (3). ATR/ATRIP coordinate DNA repair and cell cycle progression in conjunction with key regulatory proteins, such as Rad17 and the 9-1-1 complex (4). ATR associated with ATRIP can also be stimulated by topoisomerase II binding protein (TOPBP1), suggesting that ATRIP may regulate both ATR localization and activity (5).

Cyclin dependent kinase 2 (CDK2) may participate in the regulation of DNA damage response and cell cycle control through phosphorylation of ATRIP at Ser224 (6).

  1. Cortez, D. et al. (2001) Science 294, 1713-1716.
  2. Itakura, E. et al. (2004) Biochem. Biophys. Res. Commun. 323, 1197-1202.
  3. Zou, L. and Elledge, S.J. (2003) Science 300, 1542-1548.
  4. Yang, X.H. and Zou, L. (2006) Methods Enzymol. 409, 118-131.
  5. Ball, H.L. et al. (2007) Mol Cell Biol 27, 3367-77.
  6. Myers, J.S. et al. (2007) Cancer Res 67, 6685-90.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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