Not many instruments can handle characterization of all types of molecular interactions
involved in most projects in the pipeline — Monolith Pico is the exception. With both a
RED and LabelFree detector, scientists are able to take advantage of MST, the method
that Monolith Pico uses, to obtain binding affinity data for even the most challenging and
complex interactions.
If it´s important to measure protein binding in its native state, the Monolith Pico
LabelFree detector is available for use. This approach is typically needed for proteins
that cannot be labeleld, and takes advantage of a protein´s intrinsic fluorescence
generated by the presence of tryptophan and tyrosine residues. Use it to obtain K
d
s when
characterizing ligands with high nanomolar affinities that don't autofluoresce in the UV-
range. For affinities in the low nanomolar range, use it to determine EC
50
values.
For proteins that can be labeled with a RED fluorophore, Monolith Pico also includes a
RED detector that gives scientists the ability to characterize almost any type of interaction,
most notably ones involving ternary complexes or those requiring analysis in crude
extracts. Unlike other methods, this type of MST method is highly sensitive, requiring only
a small amount of sample needed to precisely determine tight binding affinities.
TECHNICAL NOTE
MONOLITH PICO
Measure binding affinities for any type of interaction —
examine a label-free or labeled target molecule at anytime
