Not that long ago, analyzing the phosphorylation of a given cellular protein could best be described as painful. If a researcher wanted to know whether a particular protein's phosphorylation status changed in response...
Phospho-specific antibodies are notorious for high levels of non-specific binding to closely
related receptors, compromising data from phosphorylation studies. Duolink® overcomes
this problem by enabling the use of dual recognition, one primary antibody against the
target protein and one primary antibody against the specific phosphorylated site.
This, together with the signal amplification of Duolink, provides a highly specific
method for signal transduction studies. In this example, visual and quantifiable
data is obtained after assaying stimulated BJ h TERT cells for phosphorylated
PDGF receptor ß.
Studies of HER2 interactions are limited by the fact that traditional
technologies do not offer the means to work on unmodified cells nor the
sensitivity to visualize individual interactions in modified cells. Duolink™
resolves these limitations and thereby provides an excellent method
for detailed and quantitative studies of HER2 interactions with putative
interacting proteins.
Studies of SMAD protein interactions are limited by the fact that traditional
technologies neither offer the means to work on unmodified cells nor the sensitivity to visualize individual interactions in modified cells. Duolink
™ resolves these limitations and thereby provides an excellent method
for detailed and qualitative studies of SMAD protein interactions. As SMAD complex formation predefines an active TGF-ß signaling pathway, we can assess the activation status of the pathway by observing SMAD complexes.