Cell Signaling Technology, Inc.

Cell Singaling Technology, Inc.

Kimberly A Lee

Roberto Polakiewicz

Albrecht Moritz

Ailan Guo

Klarisa Rikova

Ting-Lei Gu

Katherine Eleanor Crosby

John Rush

Valerie Goss

Qingfu Zeng

John Edward Rush, Ii

Peter Hornbeck

Yu Li

Charles Farnsworth

Robert Polakiewicz

An external catheter system is provided. The system includes an elongated sheath having an open upper end and an open lower end. An inflatable ring is affixed about the open upper end. In some embodiments, the inflatable ring is removably securable to the open upper end of the elongated sheath. An inflation tube is in fluid communication with an interior volume of the inflatable ring. A syringe valve is affixed to a distal end of the inflation tube, wherein the syringe valve operably connects to a syringe. Upon depression of a plunger of the syringe, air is dispensed into the inflatable ring.

External catheter system

The invention discloses a previously unidentified subset of mammalian non-small cell lung carcinomas (NSCLC) in which platelet-derived growth factor receptor alpha (PDGFR&#x3b1;) is expressed and is driving the disease, and provides methods for identifying a mammalian NSCLC tumor that belongs to a subset of NSCLC tumors in which PDGFR&#x3b1; is expressed, and for identifying a NSCLC tumor that is likely to respond to a PDGFR&#x3b1;-inhibiting therapeutic. The invention also provides methods for inhibiting the progression of a mammalian NSCLC tumor in which PDGFR&#x3b1; is expressed, and for determining whether a compound inhibits the progression of a PDGFR&#x3b1;-expressing mammalian NSCLC tumor.

Identification of non-small cell lung carcinoma (NSCLC) tumors expressing PDGFR-alpha

The invention discloses novel phosphorylation sites identified in signal transduction proteins and pathways, 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: adaptor/scaffold proteins, adhesion/extracellular matrix protein, apoptosis proteins, calcium binding proteins, cell cycle regulation proteins, chaperone proteins, chromatin, DNA binding/repair/replication proteins, cytoskeletal proteins, endoplasmic reticulum or golgi proteins, enzyme proteins, G/regulator proteins, inhibitor proteins, motor/contractile proteins, phosphatase, protease, Ser/Thr protein kinases, Protein kinase (Tyr)s, receptor/channel/cell surface proteins, RNA binding proteins, transcriptional regulators, tumor suppressor proteins, ubiquitan conjugating system proteins and proteins of unknown function.

Reagents for the detection of protein phosphorylation in signaling pathways

The invention discloses 211 novel phosphorylation sites identified in signal transduction proteins and pathways underlying Anaplastic Large Cell Lymphoma (ALCL) involving the ALK-NPM translocation/fusion, 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: Protein Kinases (including Receptor Tyrosine Kinases), Adaptor/Scaffold Proteins, Cellular Metabolism or Miscellaneous Enzymes, Oxidoreductases, Transcription Factors, Cytoskeletal Proteins, Translation Initiation Complexes, RNA Binding Proteins, Proteases, Acetyltransferases, G protein regulators/GTPases, Helicases, Apoptosis/Cell Cycle Regulation proteins, and Hydrolases.

Reagents for the detection of protein phosphorylation in anaplastic large cell lymphoma signaling pathways

The invention discloses 102 novel phosphorylation sites identified in signal transduction proteins and pathways downstream of c-Src 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: Adaptor/Scaffold proteins, Actin Binding proteins, Cytoskeletal proteins, G protein/GTPase Activating protein/Guanine Nucleotide Exchange Factor proteins, Helicases, RNA Binding proteins, Transcription/Translation Factor or Initiation Complex proteins, Cellular Metabolism Enzymes, and Vesicle proteins.

Reagents for the detection of protein phosphorylation in c-Src signaling pathways

The invention discloses 95 novel phosphorylation sites identified in signal transduction proteins and pathways downstream of the T-cell receptor, 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, Adhesion proteins, Calcium-binding proteins, Cell Cycle Regulation or Channel proteins, Chaperones, Cofactor proteins, Cytoskeletal proteins, DNA Binding proteins, G protein or GTPase Activating proteins, Ligases, Lipid Kinases and Binding proteins, Oxidoreductases, Protein Kinases, Protein Phosphatases, Receptor proteins, RNA Binding proteins, Transcription Factor/Initiation Complex proteins, Transcription Coactivator/Corepressor proteins, Translation Initiation Complex proteins, Ubitquitin Conjugating System proteins, and Vesicle proteins.

Reagents for the detection of protein phosphorylation in T-cell receptor signaling pathways

Identification of non-small cell lung carcinoma (NSCLC) tumors expressing PDGFR-&#x3b1;

The invention discloses nearly 288 novel phosphorylation sites identified in signal transduction proteins and pathways underlying human Leukemia, 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: Adaptor/Scaffold proteins, Cytoskeletal proteins, Cellular Metabolism enzymes, G Protein/GTPase Activating/Guanine Nucleotide Exchange Factor proteins, Immunoglobulin Superfamily proteins, Inhibitor proteins, Lipid Kinases, Nuclear DNA Repair/RNA Binding/Transcription proteins, Serine/Threonine Protein Kinases, Tyrosine Kinases, Protein Phosphatases, and Translation/Transporter proteins.

Reagents for the detection of protein phosphorylation in leukemia signaling pathways

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.

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Seattle, WA, United States of America

Kimberly A Lee