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NT-MO-033
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MST binding experiments
Samples were centrifuged at 14 000 x g for 10 min
at 4 °C, then loaded into Monolith NT.115 Premium
Capillaries (cat# MO-K025). Experiments with p38α
were carried out using a Monolith NT.115 system at LED
settings of 20% (RED-NHS) and 40% (RED-NHS 2nd
Generation) and high MST power. Experiments with
TEM1 were carried out using a Monolith NT.115Pico
system at LED settings of 20% (RED-NHS) and 5%
(RED-NHS 2nd Generation) and medium MST power.
Experiments with Hsp90 were carried out using
a Monolith NT.115 system at LED settings of 40%
(RED-NHS) and 40% (RED-NHS 2nd Generation)
and medium MST power. All Monolith systems were
running MO.Control so ware v1.6, and data were
analyzed at default MST-on times using MO.Affinity
Analysis so ware v2.3. All samples were prepared and
measured in triplicate.
References
1. Duhr, S., & Braun, D. (2006). Why molecules move along a
temperature gradient. Proc Natl Acad Sci U S A, 103(52), 19678–
19682.
2 P. Baaske, C. Wienken, P. Reineck, S. Duhr, D. Braun (2010). Optical
Thermophoresis for Quantifying the Buffer Dependence of Aptamer
Binding. Angew Chem Int Ed Engl, 2238-2241:
3 Underwood, D. C. et al (2000). SB 239063, a potent p38 MAP kinase
inhibitor, reduces inflammatory cytokine production, airways
eosinophil infiltration, and persistence. J. Pharmacol. Exp. Ther.
293, 281–288.