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Monolith nt 115 pico system

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The Monolith NT.115 Pico system is a lab equipment product by NanoTemper. It is designed to measure changes in the thermal stability of biomolecules. The system uses micro-scale thermophoresis technology to detect and quantify biomolecular interactions.

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Lab products found in correlation

Mo affinity analysis v2, by NanoTemper (2 mentions) Monolith nt protein labeling kit red tris nta, by NanoTemper (2 mentions) Vimentin, by Novus Biologicals (1 mentions) Monolith his tag labeling kit red tris nta 2nd generation, by NanoTemper (1 mentions)

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Monolith NT.115 (645 citations) Monolith NT.115 system (74 citations) Monolith NT.115 Pico (46 citations) NT.115 (20 citations) Monolith Pico (4 citations) NT.115 pico (3 citations)

5 protocols using monolith nt 115 pico system

1

Ybt-Fe Substrate Binding Affinity

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Substrate-binding affinity was measured using a Monolith NT.115Pico system (NanoTemper). A standard protocol was followed. Briefly, YbtPQ-LMNG with His tag was labeled with red-tris-NTA second-generation dye. For each reaction, 10 nM YbtPQ sample was mixed with Ybt-Fe at various concentrations from 0 to 50 μM. The sample was loaded into Monolith NT.115 capillaries, and microthermophoresis was performed using 20% light-emitting diode power and medium MST power. Kd values were calculated using the NanoTemper software. The reported Kd values were averages of three independent experiments.
Wang Z., Hu W, & Zheng H. (2020). Pathogenic siderophore ABC importer YbtPQ adopts a surprising fold of exporter. Science Advances, 6(6), eaay7997.
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2

Quantitative Analysis of Cap Binding

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TcEIF4E5 and TcEIF4E5-ΔC were labeled using the Monolith NT Protein Labeling Kit RED-Tris-NTA (NanoTemper Technologies) according to the supplier instructions. The concentration of labeled proteins was kept constant at 12.5 nM. The unlabeled binding partners (m7GTP or cap-4) were titrated in 1:1 dilutions with the highest final concentration of 2.5 mM. The assays were performed in triplicate in buffer containing 20 mM Tris–HCl pH 8, 100 mM NaCl, 2 mM DTT and 0.05% Tween-20. Measurements were performed in treated capillaries (NanoTemper Technologies) on a Monolith NT.115 Pico system (Nano Temper Technologies) using 20% LED and Medium IR-laser power. Data analysis were performed using MO.affinity analysis v.2.2.7 software (NanoTemper Technologies).
Reolon L.W., Vichier-Guerre S., de Matos B.M., Dugué L., Assunção T.R., Zanchin N.I., Pochet S, & Guimarães B.G. (2019). Crystal structure of the Trypanosoma cruzi EIF4E5 translation factor homologue in complex with mRNA cap-4. Nucleic Acids Research, 47(11), 5973-5987.
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3

Microscale Thermophoresis Binding Analysis

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The Microscale thermophoresis (MST) measurements were performed in treated capillaries on a Monolith NT.115 Pico system (Nano Temper Technologies) using 20% LED and Medium IR-laser power. BGLA and K44A mutant were labeled using the Monolith NT Protein Labeling Kit RED-Tris-NTA (NanoTemper Technologies) according to the supplier instructions. The concentration of labeled proteins was kept constant at 12.5 nM in the assays. The unlabeled binding partner (G6P) was titrated in 1:1 dilutions with the highest concentration of 200 mM. The assays were performed in triplicate in buffer containing 50 mM Hepes pH 7.0. Data analysis were performed using MO affinity analysis v.2.2.7 software (NanoTemper Technologies). Kd values were obtained from compound concentration-dependent changes in normalized fluorescence (Fnorm) of BGLA or K44A mutant. The data were fitted with the help of the quadratic fitting formula derived from the law of mass action.
Gomes A.A., da Silva G.F., Lakkaraju S.K., Guimarães B.G., MacKerell AD J.r, & Magalhães M.D. (2021). INSIGHTS INTO GLUCOSE-6-PHOSPHATE ALLOSTERIC ACTIVATION OF β-GLUCOSIDASE A. Journal of chemical information and modeling, 61(4), 1931-1941.
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4

Multivalent ASCPYD Polymerization Assay

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MST was performed according to established protocols (26 (link)), with minor modifications. The buffer was changed to 1x PBS and glutathione was added to a final concentration of 13 mM to mimic intracellular conditions. In short, a dilution series was prepared with unlabelled ASCPYD and mixed with Atto488-labeled ASCPYD, TEV Protease to start polymerisation, and either plasma-purified or recombinant C4BP in their respective concentrations. The mixture was filled into capillaries, incubated and measured with 60% MST-power using the Monolith NT.115Pico system (NanoTemper Technologies, Munich, Germany) under control of NT Software (version 2.2.1).
Bierschenk D., Papac-Milicevic N., Bresch I.P., Kovacic V., Bettoni S., Dziedzic M., Wetsel R.A., Eschenburg S., Binder C.J., Blom A.M, & King B.C. (2023). C4b-binding protein inhibits particulate- and crystalline-induced NLRP3 inflammasome activation. Frontiers in Immunology, 14, 1149822.
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5

Quantifying Protein-Protein Interactions

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Three independent MST experiments were performed with His-tagged BspC labelled using the Monolith His-Tag Labeling Kit RED-tris-NTA 2nd Generation (NanoTemper Technologies) according to manufacturer’s instructions. The concentration of labelled BspC was kept constant at 10nM. Vimentin was purchased from Novus Biologicals and titrated in 1:1 dilutions to obtain a series of 16 titrations ranging in concentration from 20 μM to 0 μM. Measurements were performed in standard capillaries with a Monolith NT.115 Pico system at 20% excitation power and 40% MST power (NanoTemper Technologies).
Deng L., Spencer B.L., Holmes J.A., Mu R., Rego S., Weston T.A., Hu Y., Sanches G.F., Yoon S., Park N., Nagao P.E., Jenkinson H.F., Thornton J.A., Seo K.S., Nobbs A.H, & Doran K.S. (2019). The Group B Streptococcal surface antigen I/II protein, BspC, interacts with host vimentin to promote adherence to brain endothelium and inflammation during the pathogenesis of meningitis. PLoS Pathogens, 15(6), e1007848.
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