Rachel Friedman Ohana

TL;DR: The utility of this modular protein tagging system for cellular imaging and protein immobilization is demonstrated by analyzing multiple molecular processes associated with NF-kappaB-mediated cellular physiology, including imaging of subcellular protein translocation and capture of protein--protein and protein--DNA complexes.

TL;DR: A broadly applicable method using bioluminescence resonance energy transfer (BRET) to reveal the binding characteristics of a drug with selected targets within intact cells to demonstrate a novel application of BRET for assessing target engagement within the complex milieu of the intracellular environment.

TL;DR: An energy transfer technique is reported that enabled the first broad-spectrum, equilibrium-based approach to quantitatively profile target occupancy and compound affinity in live cells and revealed improved target selectivity compared with biochemical measurements.

TL;DR: A novel protein tag engineered to enhance expression and solubility of recombinant proteins and to provide efficient protein purification coupled with tag removal, designed to bind rapidly and covalently with a unique synthetic linker to achieve an essentially irreversible attachment.

TL;DR: HaloTag® (HT7), a genetic fusion tag based on a modified haloalkane dehalogenase designed and engineered to overcome the limitation of affinity tags by forming a high affinity, covalent attachment to a binding ligand, is described.