Dergi
/
Biyokimya
/
Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells
JoVE Journal
Biyokimya
Bu içeriği görüntülemek için JoVE aboneliği gereklidir.  Oturum açın veya ücretsiz deneme sürümünü başlatın.
JoVE Journal Biyokimya
Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells

Time-resolved Förster Resonance Energy Transfer Assays for Measurement of Endogenous Phosphorylated STAT Proteins in Human Cells

DOI:
10.3791/62915-v

•

07:12 min

•

September 09, 2021

•

, ,
1BioAuxilium Research

Bölümler

  • 00:05Introduction
  • 01:02Stimulator or Inhibitor Titration Using the Two-Plate Assay Protocol with Adherent Cells
  • 04:33Results: Two-Plate and One-Plate Detection of STAT Proteins in Adherent and Suspension Cell Lines, and Intraplate Variability Study
  • 06:40Conclusion

Özet

Otomatik Çeviri

Otomatik Çeviri

Time-resolved Förster resonance energy transfer cell-based assay protocols are described for the simple, specific, sensitive, and robust quantification of endogenous phosphorylated signal transducer and activator of transcription (STAT) 1/3/4/5/6 proteins in cell lysates in a 384-well format.

Etiketler

Time-resolved FRETTR-FRETSTAT ProteinsJAK/STAT SignalingImmunoassayCell CultureCell StimulationCell LysisPhosphatase InhibitorsHigh-throughput ScreeningPharmacological Characterization

Article

Embed

ÇALMA LİSTESİNE EKLE

Usage Statistics

İlgili Videolar

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Isolation and Respiratory Measurements of Mitochondria from Arabidopsis thaliana

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Transverse Sectioning of Mature Rice (Oryza sativa L.) Kernels for Scanning Electron Microscopy Imaging Using Pipette Tips as Immobilization Support

Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens

Fast Grid Preparation for Time-Resolved Cryo-Electron Microscopy

Read Article