Cell Signaling Technology, Inc.

Robert Polakiewicz

Ailan Guo

Klarisa Rikova

Albrecht Moritz

Kimberly A Lee

Yu Li

Charles Farnsworth

Hong Ruan

Mark Livingstone

The invention discloses two novel phosphorylation sites in human ATR kinase, serine 428 (Ser428) and serine 2317 (Ser2317) respectively, and provides reagents, including antibodies and AQUA peptides, that selectively bind to and/or detect ATR only when phosphorylated at one or more of these respective sites, but do not bind to ATR when not phosphorylated at these respective sites. Also provided are methods for determining the phosphorylation of ATR kinase in a biological sample, by using a detectable reagent that binds to ATR only when phosphorylated at Ser428 and/or Ser2317. Kits comprising the ATR (Ser428, Ser2317)-specific reagents of the invention are also provided.

Reagents for the detection of phosphorylated ATR kinase (Ser 428) and uses thereof

The invention discloses 168 novel phosphorylation sites identified in signal transduction proteins and pathways downstream of, and including, EGFR kinase, and provides phosphorylation-site specific antibodies and heavy-isotope labeled peptides (AQUA peptides) for the selective detection and quantification of these phosphorylated sites/proteins, as well as methods of using the reagents for such purpose. Among the phosphorylation sites identified are sites occurring in the following protein types: Actin Binding proteins, Adaptor/Scaffold proteins, Calcium-Binding Proteins, Cell Cycle Regulation proteins, Cytoskeletal proteins, DNA Binding and Replication Proteins, GTPase Activating proteins, Guanine Nucleotide Exchange Factor proteins, Lipid Kinases, Receptor Tyrosine Kinases, Receptor Tyrosine Kinase ligands, Protein Kinases, Receptor and Protein Phosphatases, Transcription Factor proteins, Tumor Suppressor proteins, and Vesicle proteins.

Reagents for the detection of protein phosphorylation in EGFR-signaling pathways

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Lexington, MA, United States of America

Robert Polakiewicz