Biosensor interaction experiments

Measure binding of small molecules or proteins to a protein of interest on a biosensor surface

How it works:
The lysate containing the protein of interest expressed as a SNAP-tag fusion is added to a biosensor chip previously coated with SNAP-tag substrate. The protein of interest immobilizes itself covalently through the SNAP-tag. After washing, binding experiments can be performed without drift.
Advantages:
- Oriented immobilization without prior purification ensures maximal functionality of the protein of interest.
- Covalent binding to the chip eliminates drifts from slow release of protein.



Self-immobilization of SNAP-tag fusion proteins on surfaces. Biacore data showing the specific immobilization of GST-SNAP out of a lysate directly onto the sensor chip.

Products:

CBG-NH2

BG-PEG-NH2

Literature:

Publications:
Kufer S.K. et al: "Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy.", Eur Biophys J (2005), 35(1), pp. 72-78
Huber W. et al.:"SPR-based interaction studies with small molecular weight ligands using hAGT fusion proteins." Analytical Biochemistry 333(2) (2004), pp280-288.
Kindermann M. et al. "Covalent and selective immobilization of fusion proteins." JACS 125(26) (2003), pp. 7810-7811.