Biotinylated Kinases are now available from Carna Biosciences! These important reagents are best suited for the study of binding affinity and other kinase-molecule interactions on devices measuring Surface Plasmon Resonance (SPR), BioLayer Interferometry (BLI) and other similar values. They can also be utilized in homogenous proximity-based binding assays such as TR-FRET to interrogate inhibitor binding affinity, determine on-off rates, and measure binding kinetics.
The immobilization of target proteins onto sensor surfaces without impairing their structure and activity can be quite a challenging step in small molecule drug discovery.
Carna' s in-house single-site specifically biotinylated kinases can easily facilitate this immobilization and lead to the acquisition of real-time and accurate data for quick evaluation in your programs!
Advantages of Carna’s Biological Biotinylation
- Kinases are labeled with a single biotin on the N-terminus
- Easy-to-use - no additional labeling required
- Native, catalytically active kinase domains.
- High quality human proteins produced in Baculovirus expression system (insect cells)
- Stable Activity
- Some kinases are available with pre-activation by ATP treatment, or unactivated (no ATP pre-treatment).
- Single vs. multiple biotin molecules, which can possibly interfere with the ATP binding site following chemical biotinylation.
- Preserved kinase activity and structure, which can be altered with chemical modification.
- No additional purification is required (for excluding non-reacted biotin).
Reference：Quick Evaluation of Kinase Inhibitors by Surface Plasmon Resonance
Using Single-Site Specifically Biotinylated Kinases
Daisuke Kitagawa, Masaki Gouda and Yasuyuki Kirii
J Biomol Screen 2014 19: 453 originally published online 30 September 2013
Please feel free to contact us for more details.