Log In Sign up
The largest database of trusted experimental protocols

Pr thermcontrol v2

Manufactured by NanoTemper
Visit Supplier

PR.ThermControl v2.0.4 is a lab equipment product by NanoTemper. It is a temperature control device that regulates and monitors the temperature of samples during experiments.

Automatically generated - may contain errors

Lab products found in correlation

Prometheus nt 48, by NanoTemper (6 mentions) Prometheus nt 48 nanodsf, by NanoTemper (2 mentions) Prism 9, by GraphPad (2 mentions) Hbs p, by Cytiva (2 mentions) Prometheus nt 48 instrument, by NanoTemper (1 mentions)

Spelling variants of this product

PR.ThermControl (16 citations)

9 protocols using pr thermcontrol v2

1

Thermal Stability Evaluation of PPP2R1A

Check if the same lab product or an alternative is used in the 5 most similar protocols
The thermal stability of PPP2R1A in both NMR and ITC buffers with different percentage of DMSO (from 0% to 40%) was evaluated by following the changes in the intrinsic fluorescence ratio (350/330 nm) as a function of the temperature. The experiments were run in a Prometheus NT.48 nanoDSF (NanoTemper Technologies). Ten microliters of the protein samples at 10 μM were measured in triplicates with a temperature ramp set to 1°C/min from 20°C to 80°C using standard treated capillaries (NanoTemper Technologies (#PR‐C002)). The PR. ThermControl v2.1.6 software (NanoTemper Technologies) was used for data acquisition and data analysis.
Vit G., Duro J., Rajendraprasad G., Hertz E.P., Holland L.K., Weisser M.B., McEwan B.C., Lopez‐Mendez B., Sotelo‐Parrilla P., Jeyaprakash A.A., Montoya G., Mailand N., Maeda K., Kettenbach A., Barisic M, & Nilsson J. (2022). Chemogenetic profiling reveals PP2A‐independent cytotoxicity of proposed PP2A activators iHAP1 and DT‐061. The EMBO Journal, 41(14), e110611.
+ Open protocol
+ Expand
2

Thermal Stability of PPP2R1A Protein

Check if the same lab product or an alternative is used in the 5 most similar protocols
The thermal stability of PPP2R1A in both NMR and ITC buffers with different percentage of DMSO (from 0% to 40%) was evaluated by following the changes in the intrinsic fluorescence ratio (350/330 nm) as a function of the temperature. The experiments were run in a Prometheus NT.48 nanoDSF (NanoTemper Technologies). 10 μl of the protein samples at 10 μM were measured in triplicates with a temperature ramp set to 1 °C/min from 20 °C-80 °C using standard treated capillaries (NanoTemper Technologies (#PR-C002)). The PR.ThermControl v2.1.6 software (NanoTemper Technologies) was used for data acquisition and data analysis.
Vit G., Duro J., Rajendraprasad G., Hertz E.P.T., Holland L.K., Weisser M., McEwan B.C., López‐Méndez B., Montoya G., Mailand N., Maeda K., Kettenbach A.N., Barišić M., & Nilsson J. (2021). Cellular toxicity of iHAP1 and DT-061 does not occur through PP2A-B56 targeting.
+ Open protocol
+ Expand
3

Thermal Stability Analysis of Proteins

Cited 2 times
Check if the same lab product or an alternative is used in the 5 most similar protocols
Measurements were performed in triplicates on a Prometheus NT.48 (NanoTemper), at 0.2 mg/ml, between 20 and 95 °C. Data was exported using PR.ThermControl v2.0.4 (NanoTemper), and fitted using Eq. 2 as described above. Tonset was calculated using MoltenProt at the eSPC online data analysis platform 37 (link),59 (link).
Hagströmer C.J., Hyld Steffen J., Kreida S., Al-Jubair T., Frick A., Gourdon P, & Törnroth-Horsefield S. (2023). Structural and functional analysis of aquaporin-2 mutants involved in nephrogenic diabetes insipidus. Scientific Reports, 13, 14674.
+ Open protocol
+ Expand
4

Characterizing Protein Thermal Stability via NanoDSF

Check if the same lab product or an alternative is used in the 5 most similar protocols
Nano Differential Scanning Fluorescence (NanoDSF) was performed with a Prometheus NT.48 instrument (NanoTemper Technologies GmbH, München, Germany). Purified OhLys variants (in either 250 mM Na-acetate, pH 4.7, or 20 mM tris(hydroxymethyl)aminomethane, pH 8.0) were loaded into nanoDSF standard grade capillaries (NanoTemper Technologies GmbH; catalogue number PR-C002) through capillary action. Three capillaries were filled for each sample. The capillaries were then placed into the instrument (up to 48 single capillaries can be loaded in a single run) and the laser intensity required for optimum signal generation was determined. The samples were run with the following experimental setting: temperature slope 2 °C/minute, start temperature 20 °C and end temperature 95 °C. The data were analysed using the software supplied with the instrument (PR.ThermControl v2.0.4, NanoTemper Technologies GmbH) and the Tm (for the ratio 350 nm/330 nm).
Taylor E.J., Skjøt M., Skov L.K., Klausen M., De Maria L., Gippert G.P., Turkenburg J.P., Davies G.J, & Wilson K.S. (2019). The C-Type Lysozyme from the upper Gastrointestinal Tract of Opisthocomus hoatzin, the Stinkbird. International Journal of Molecular Sciences, 20(22), 5531.
+ Open protocol
+ Expand
5

Nanodifferential Scanning Fluorimetry for Protein Stability

Check if the same lab product or an alternative is used in the 5 most similar protocols
The nanodifferential scanning fluorimetry (nanoDSF) is based on intrinsic
protein fluorescence using aromatic residues (tryptophan, tyrosine).
nanoDSF measures the changes in the intrinsic fluorescence intensity
ratio (350:330 nm), as a function of temperature.
The Prometheus
NT.48 instrument (NanoTemper Technologies) was used to determine the
melting temperatures of SLC15A4 in the presence and absence of compounds.
The capillaries (high sensitivity) were filled with 10 μL of
sample containing 0.2 mg mL–1 SLC15A4 diluted in
purification buffer (refer to protein purification). A temperature
gradient of 1 °C min–1 from 25 °C to 85
°C was applied, and the ratio of intrinsic protein fluorescence
at 350:330 nm was recorded. Small molecules were added to the final
concentration of 50 μM with a DMSO content of 5% (v/v). Protein
stability was not affected by DMSO additions up to 6% (v/v). Apo protein
was measured in quadruplets, and all measurements containing compounds
were performed in duplicate. A control compound was included during
every assay run to monitor the assay performance. The protein stabilization
upon small molecule addition was recorded as dTm in °C [Tm(compound) – Tm(apo)]. The nanoDSF data analysis was performed
using PR.ThermControl v2.0.4 software (NanoTemper Technologies).
Thomas J.R., Shelton C I.V., Murphy J., Brittain S., Bray M.A., Aspesi P., Concannon J., King F.J., Ihry R.J., Ho D.J., Henault M., Hadjikyriacou A., Neri M., Sigoillot F.D., Pham H.T., Shum M., Barys L., Jones M.D., Martin E.J., Blechschmidt A., Rieffel S., Troxler T.J., Mapa F.A., Jenkins J.L., Jain R.K., Kutchukian P.S., Schirle M, & Renner S. (2024). Enhancing the Small-Scale Screenable Biological Space beyond Known Chemogenomics Libraries with Gray Chemical Matter—Compounds with Novel Mechanisms from High-Throughput Screening Profiles. ACS Chemical Biology, 19(4), 938-952.
+ Open protocol
+ Expand
6

Thermal Stability Profiling of Muramidases

Check if the same lab product or an alternative is used in the 5 most similar protocols
Nano Differential Scanning Fluorescence (nanoDSF) was performed on eight of the muramidases with a Prometheus NT.48 instrument (NanoTemper Technologies GmbH, München, Germany). Purified samples (in either 50 mM Na-acetate, pH 3.0, or 50 mM Na-acetate, pH 5.0) were loaded into nanoDSF standard grade capillaries (NanoTemper Technologies GmbH) through capillary action. Three capillaries were filled for each sample, placed into the instrument (up to 48 single capillaries can be loaded in a single run) and the laser intensity required for optimum signal generation was determined. The samples were run with the following experimental setting: temperature slope 2°C/minute, start temperature 20°C and end temperature 95°C. The data were analysed using the software supplied with the instrument (PR.ThermControl v2.0.4, NanoTemper Technologies GmbH) and the melting point, Tm (°C), (for the ratio 350 nm/330 nm) was determined.
Moroz O.V., Blagova E., Taylor E., Turkenburg J.P., Skov L.K., Gippert G.P., Schnorr K.M., Ming L., Ye L., Klausen M., Cohn M.T., Schmidt E.G., Nymand-Grarup S., Davies G.J, & Wilson K.S. (2021). Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. PLoS ONE, 16(3), e0248190.
+ Open protocol
+ Expand
7

Thermal Stability of LDHD Mutants

Check if the same lab product or an alternative is used in the 5 most similar protocols
The protein solution (wild-type and mLDHD mutants) was diluted with the storage buffer to a concentration of 1 mg/ml. The sample (50 μl) was loaded with high precision quartz glass capillary (Shanghai Yuanyi Biotechnology). Protein thermostability was determined using a Prometheus NT.48 instrument (NanoTemper Technologies). The temperature range was 25–95 °C with a rise of 1 °C per min. Fluorescence intensities were measured at 330 nm and 350 nm. Data were analyzed using PR.ThermControl v2.3.1 (NanoTemper Technologies). All experiments were performed in triplicates using distinct samples, and the Tm values were the averages of the triplicate measurements with the standard errors.
Jin S., Chen X., Yang J, & Ding J. (2023). Lactate dehydrogenase D is a general dehydrogenase for D-2-hydroxyacids and is associated with D-lactic acidosis. Nature Communications, 14, 6638.
+ Open protocol
+ Expand
8

Thermal Denaturation Assay of p110α/p85α

Check if the same lab product or an alternative is used in the 5 most similar protocols
Thermal denaturation was followed using intrinsic protein fluorescence measured with the NanoTemper Prometheus NT48 instrument (Nanotemper Technologies, München, Germany). Samples in HBS-P (Cytiva) supplemented with 5% (v/v) DMSO containing 3 μM full length p110α/p85α and a 1:2 dilution series of 1938 (from 440 μM to 13.8 nM) were loaded into standard capillaries and heated at 2 °C/min from 15 to 95 °C. The first derivative of the fluorescence emission ratio 350/330 nm were analyzed using the PR.ThermControl v2.3.1 (NanoTemper), to define the Tm. Independent experiments using the same protein and compound stocks were performed in triplicate. Data were fitted using Prism 9.4.1 (GraphPad Software Inc). Dissociation constants were calculated using fits to a single-site ligand depletion model: T=T0+(T1−T0){([CT]+[PT]+[KD])−([CT]+[PT]+KD)2−4[CT][PT]}2[PT] where T0 and T1 are the Tm in the absence of titrating compound and at saturation respectively, [PT] and [CT] are the total concentrations of protein and compound respectively and KD is the dissociation constant.
Gong G.Q., Bilanges B., Allsop B., Masson G.R., Roberton V., Askwith T., Oxenford S., Madsen R.R., Conduit S.E., Bellini D., Fitzek M., Collier M., Najam O., He Z., Wahab B., McLaughlin S.H., Chan A.E., Feierberg I., Madin A., Morelli D., Bhamra A., Vinciauskaite V., Anderson K.E., Surinova S., Pinotsis N., Lopez-Guadamillas E., Wilcox M., Hooper A., Patel C., Whitehead M.A., Bunney T.D., Stephens L.R., Hawkins P.T., Katan M., Yellon D.M., Davidson S.M., Smith D.M., Phillips J.B., Angell R., Williams R.L, & Vanhaesebroeck B. (2023). A small molecule PI3Kα activator for cardioprotection and neuroregeneration. Nature, 618(7963), 159-168.
+ Open protocol
+ Expand
9

Thermal Denaturation Assay of p110α/p85α

Check if the same lab product or an alternative is used in the 5 most similar protocols
Thermal denaturation was followed using intrinsic protein fluorescence measured with the NanoTemper Prometheus NT48 instrument (Nanotemper Technologies, München, Germany). Samples in HBS-P (Cytiva) supplemented with 5% (v/v) DMSO containing 3 μM full length p110α/p85α and a 1:2 dilution series of 1938 (from 440 μM to 13.8 nM) were loaded into standard capillaries and heated at 2 °C/min from 15 to 95 °C. The first derivative of the fluorescence emission ratio 350/330 nm were analyzed using the PR.ThermControl v2.3.1 (NanoTemper), to define the Tm. Independent experiments using the same protein and compound stocks were performed in triplicate. Data were fitted using Prism 9.4.1 (GraphPad Software Inc). Dissociation constants were calculated using fits to a single-site ligand depletion model: T=T0+(T1−T0){([CT]+[PT]+[KD])−([CT]+[PT]+KD)2−4[CT][PT]}2[PT] where T0 and T1 are the Tm in the absence of titrating compound and at saturation respectively, [PT] and [CT] are the total concentrations of protein and compound respectively and KD is the dissociation constant.
Gong G.Q., Bilanges B., Allsop B., Masson G.R., Roberton V., Askwith T., Oxenford S., Madsen R.R., Conduit S.E., Bellini D., Fitzek M., Collier M., Najam O., He Z., Wahab B., McLaughlin S.H., Chan A.E., Feierberg I., Madin A., Morelli D., Bhamra A., Vinciauskaite V., Anderson K.E., Surinova S., Pinotsis N., Lopez-Guadamillas E., Wilcox M., Hooper A., Patel C., Whitehead M.A., Bunney T.D., Stephens L.R., Hawkins P.T., Katan M., Yellon D.M., Davidson S.M., Smith D.M., Phillips J.B., Angell R., Williams R.L, & Vanhaesebroeck B. (2023). A small molecule PI3Kα activator for cardioprotection and neuroregeneration. Nature, 618(7963), 159-168.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!