• Home
  • Research areas
    • ADME-Tox
    • Biomarkers
    • Cell Biology and Signalling
    • Cell Sourcing – Cell Culture Technologies
    • Drug Discovery
    • Gene Expression – Molecular Biology
    • Stem Cells
    • Supplying Discovery Tools
  • Contact us
  • Meet the authors
  • Facebook
  • Google+
  • LinkedIn
  • Twitter
  • YouTube
Home
Research areas
    ADME-Tox
    Biomarkers
    Cell Biology and Signalling
    Cell Sourcing - Cell Culture Technologies
    Drug Discovery
    Gene Expression - Molecular Biology
    Stem Cells
    Supplying Discovery Tools
Contact us
Meet the authors
tebu-bio's blog - Acting and reacting in life sciences and biotechnologies
  • Home
  • Research areas
    • ADME-Tox
    • Biomarkers
    • Cell Biology and Signalling
    • Cell Sourcing – Cell Culture Technologies
    • Drug Discovery
    • Gene Expression – Molecular Biology
    • Stem Cells
    • Supplying Discovery Tools
  • Contact us
  • Meet the authors
Gene Expression - Molecular Biology

BioID proximity-dependent biotinylation studies

17/06/2015 by Mark Livingstone No Comments

In 2012, Roux et al. published a nice paper, that received no less than four article recommendations from F1000 researchers. The paper described a method for tracking the interaction partners a protein has had within a cell (a history of its interacting partners). The method, called BioID, is based on proximity-dependent biotinylation of proteins by a promiscuous biotin ligase mutant BirA (R118G), which is fused to your protein of interest. After an overnight incubation with biotin, cells can be subjected to harsh lysis and biotinylated proteins can be isolated and identified by mass spectroscopy to determine the proteins that had come into contact with the chimeric BirA (R118G) protein. This method is a bit different from standard co-IP or pull-down experiments, because it allows one to identify proteins who interact transiently or weakly with the protein of interest. Also, due to the strong biotin-avidin binding affinity, harsh washes can greatly reduce background protein binding.

Continue reading
tebu-bio

LAB SERVICES OUTSOURCING

• Protein production

• Plasmid Preps

• 3D Cell Culture
LEARN MORE

Most popular posts

  • HeLa cells: Origin of this important cell line in life science research
  • From RUO to IVD - the acronym guide to reagents' intended use
  • How to choose the perfect buffer to get a pure, stabilised, functional protein
  • Lipid-Ligand interaction tools: lipids are not scary intermediates anymore
  • Differentiate between Apoptosis, Necroptosis, Autophagy & Ferroptosis
My Tweets

Top contributors

Dimitri Szymczak, PhD
Dimitri Szymczak, PhD
  • New ATM and ATR inhibitor biomarker – How to study key sensors of DNA damage
  • Get closer to the real Host Cell Protein (HCP) quantity
Frédéric Samazan
Frédéric Samazan
  • Lympholyte®: The ideal tool for simple and viable lymphocytes isolation
  • CAR T-Cell therapy: new hope for Immunotherapy and Cancer treatment
Isabelle Nobiron
Isabelle Nobiron
  • Proteomics Biostats: get the most out of your array data
  • Hepatic Hyaluronan Content increased by Alcohol Consumption in Patients with Liver Steatosis
Isabelle Topin, PhD
Isabelle Topin, PhD
  • Monoclonal antibodies – all you need to know about antibody generation
  • Tips and Tricks: how to increase unstable protein expression in E. Coli
Philippe Fixe, PhD
Philippe Fixe, PhD
  • 10 Human Immune Checkpoint biomarkers quantified simultaneously
  • 3D cell culture: discover the new VitroGel™ 3D Hydrogel system

Copyright © 2018 - tebu-bio - visit our main website at tebu-bio.com