JAK-STAT Signalling : Methods and Protocols /

Detalles Bibliográficos
Autor Corporativo: SpringerLink (Online service)
Otros Autores: Nicholson, Sandra E. (Editor ), Nicola, Nicos A. (Editor )
Formato: eBook
Lenguaje:English
Publicado: Totowa, NJ : Humana Press : Imprint: Humana, 2013.
Edición:1st ed. 2013.
Colección:Methods in Molecular Biology, 967
Materias:
Tabla de Contenidos:
  • Analysis of Janus Tyrosine Kinase Phosphorylation and Activation
  • Co-Immunoprecipitation Protocol to Investigate Cytokine Receptor Associated Proteins e.g. Janus Kinases or Other Associated Signaling Proteins
  • In Vitro JAK Kinase Activity and Inhibition Assays
  • Quantitative Analysis of JAK Binding using Isothermal Titraion Calorimetry and Surface Plasmon Resonance
  • Determination of Protein Turnover Rates in the JAK/STAT Pathway using a Radioactive Pulse-Chase Approach
  • Designing RNAi Screens to Identify JAK/STAT Pathway Components
  • The Use of JAK-Specific Inhibitors as Chemical Biology Tools
  • Methods for Detecting Mutations in the Human JAK2 Gene
  • Detection of Activated STAT Proteins
  • Detection of Activated STAT Species Using Electrophoretic Mobility Shift Assay (EMSA) and Potential Pitfalls Arising from the Use of Detergents
  • Flow Cytometric Analysis of STAT Phosphorylation
  • Acetylation of Endogenous STAT Proteins
  • Detection and Cellular Localization of Phospho-STAT2 in the Central Nervous System by Immunohistochemical Staining
  • Nuclear Trafficking of STAT Proteins Visualized by Live Cell Imaging
  • Characterization of STAT Self-Association by Analytical Ultracentrifugation
  • Constitutively Active STAT5 Constructs
  • Analysis of Suppressor of Cytokine Signalling (SOCS) Gene Expression by Real-Time Quantitative PCR
  • Detection of Endogenous SOCS1 and SOCS3 Proteins by Immunoprecipitation and Western Blot Analysis
  • In vitro Ubiquitination of Cytokine Signaling Components
  • Production and Crystallization of Recombinant JAK Proteins
  • Bacterial Expression, Purification and Crystallization of Tyrosine Phosphorylated STAT Proteins.