His-Tag Protein Binding

Tris-NTA.: Proteomics is dependent on reliable and sensitive detection and labeling of tagged protein, such as those bearing the 6x His-tag. However, considering the low affinity of currently available chelators used for protein binding limiting the sensitivity of many applications for selective, site-specific conjugation of proteins. This issue can be addressed by using a superior His-tag protein ligand for the reversible binding of proteins and cell surfaces.

The binding affinity approximately four orders of magnitude higher than monovalent metal ion chelators (such as nitrilotriacetic acid and iminodiacetic acid), ensures Tris-NTA's increased sensitivity in a western hybridization, biosensor analysis, functional protein analysis, protein purification and many other applications.

Some of the broad advantages are:
1. Extremely high sensitivity
2. Diversified application — for reversible binding of proteins, oligosaccharides, fluorophores, lipids, etc.
3. Minimalistic effects on protein functioning — for greater flexibility in functional assays