How to eliminate non-specific binding?

Non-specific binding can be eliminated using these strategies: 

1. Adjust buffer pH: The pH of both the running buffer and analyte solution affects non-specific binding by influencing the charge of biomolecules. Matching the pH to the isoelectric point of your protein or neutralizing the sensor surface will help eliminate non-specific binding.
2. Increase salt concentration: Higher salt (NaCl) concentrations shield charged proteins from interacting with surfaces, reducing non-specific binding caused by charge-based interactions.
3. Use buffer additives: Add bovine serum albumin (BSA) to buffer and sample solutions when using a protein as your analyte. BSA shields the analyte from interactions with charged surfaces as well as non-specific protein interactions. BSA is typically added at 1% concentration but this can differ from one experiment to another. 
4. Add surfactants: Introducing low concentrations of a non-ionic surfactant can help if hydrophobic interactions in your system are causing the non-specific binding. Non-ionic surfactants disrupt hydrophobic interactions between the analyte and sensor surface, reducing non-specific binding. They also prevent analyte binding to tubing and container walls.

Consider the characteristics of your analyte and ligand, such as isoelectric point, charge, size, and composition, in order to choose the best method for eliminating non-specific binding.