Nt 48 nano dsf instrument

Manufactured by NanoTemper

The NT.48 nano-DSF instrument is a compact and reliable device designed for high-throughput thermal stability analysis. It utilizes the nanoDSF (Differential Scanning Fluorimetry) technique to measure the thermal unfolding of proteins and protein complexes. The instrument can precisely monitor changes in the intrinsic fluorescence of a sample as it is heated, providing valuable insights into a protein's thermal stability and folding behavior.

Automatically generated - may contain errors

Lab products found in correlation

Tbs buffer, by Thermo Fisher Scientific (1 mentions) Nanodsf capillaries, by NanoTemper (1 mentions) Pr c006, by NanoTemper (1 mentions)

Spelling variants of this product

NT.48 (12 citations)

5 protocols using nt 48 nano dsf instrument

Thermal Stability of LRRK1 Mutants

Check if the same lab product or an alternative is used in the 5 most similar protocols

Thermal stability was measured using the Prometheus NT.48 nano-DSF instrument (NanoTemper). LRRK1 or the relevant mutant in the buffer 20 mM Tris, 150 mM NaCl, 5 mM MgCl₂, 0.0008% Tween-80 pH 8.3, at a concentration of 0.1 mg/mL was loaded into a nanoDSF glass capillary. Thermal unfolding was measured at a heating rate at 1 °C, protein melting temperature was calculated from the first derivative of the ratio of tryptophan fluorescence at 330 nm and 350 nm.

Metcalfe R.D., Martinez Fiesco J.A., Bonet-Ponce L., Kluss J.H., Cookson M.R, & Zhang P. (2023). Structure and regulation of full-length human leucine-rich repeat kinase 1. Nature Communications, 14, 4797.

+ Open protocol

+ Expand

Thermal Stability Profiling of Protein Variants

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Prometheus NT.48 NanoDSF instrument (NanoTemper Technologies) was used for the DSF experiments, as described previously.⁶⁰ (link) GPC, GPC-I53-50A and GPC-I53-50NP samples were diluted to 1 mg/mL in the TBS buffer (Alfa Aesar) and ∼10 μL of each diluted sample (in duplicates) was loaded into NanoDSF capillaries (NanoTemper Technologies). The temperature was raised from 20°C to 95°C at 1°C/min rate. The T_m value was determined from the first derivative curves using the NT.48 NanoDSF instruments software. The average value from the duplicate measurements is reported as the T_m value in the manuscript.

Brouwer P.J., Antanasijevic A., Ronk A.J., Müller-Kräuter H., Watanabe Y., Claireaux M., Perrett H.R., Bijl T.P., Grobben M., Umotoy J.C., Schriek A.I., Burger J.A., Tejjani K., Lloyd N.M., Steijaert T.H., van Haaren M.M., Sliepen K., de Taeye S.W., van Gils M.J., Crispin M., Strecker T., Bukreyev A., Ward A.B, & Sanders R.W. (2022). Lassa virus glycoprotein nanoparticles elicit neutralizing antibody responses and protection. Cell Host & Microbe, 30(12), 1759-1772.e12.

+ Open protocol

+ Expand

Thermal Stability Analysis of Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols

Melt curves utilizing the intrinsic tryptophan and tyrosine fluorescence of the protein sample were recorded using a Prometheus NT.48 nano-DSF instrument (NanoTemper technologies). Protein was diluted to 0.2 mg/ml in binding buffer (as above) and recorded in nano-DSF grade standard capillaries at 50% fluorescence intensity between 15 and 95 °C with a temperature ramp rate of 2 °C/min.

Stowell J.A., Wagstaff J.L., Hill C.H., Yu M., McLaughlin S.H., Freund S.M, & Passmore L.A. (2018). A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. The Journal of Biological Chemistry, 293(24), 9210-9222.

+ Open protocol

+ Expand

Determining SOSIP Trimer Tm by NanoDSF

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Prometheus NT.48 NanoDSF instrument (NanoTemper Technologies) was used for all the T_m determination experiments, as described previously^{27 (link)}. SOSIP trimer and SOSIP-I53-50NP samples (in triplicates) were diluted to 0.35 mg/mL in TBS and loaded into NanoDSF capillaries. The temperature was increased from 20–95 °C at a rate of 1 °C/min. Instrument software was used to calculate the 1st derivative curve and the location of the maximum was taken as the T_m value.

Brouwer P.J., Antanasijevic A., de Gast M., Allen J.D., Bijl T.P., Yasmeen A., Ravichandran R., Burger J.A., Ozorowski G., Torres J.L., LaBranche C., Montefiori D.C., Ringe R.P., van Gils M.J., Moore J.P., Klasse P.J., Crispin M., King N.P., Ward A.B, & Sanders R.W. (2021). Immunofocusing and enhancing autologous Tier-2 HIV-1 neutralization by displaying Env trimers on two-component protein nanoparticles. NPJ Vaccines, 6, 24.

+ Open protocol

+ Expand

Comparative Analysis of rAAV Thermal Stability

Check if the same lab product or an alternative is used in the 5 most similar protocols

Purified rAAV capsids of various serotypes produced by each manufacturing platform were compared for their denaturing thermal stability. 10 μL of undiluted rAAV of each lot was loaded into a high-sensitivity capillary (NanoTemper, catalog no. PR-C006) and run on a NanoTemper Prometheus NT.48 nanoDSF instrument. Thermal denaturation programs were run with a 1°C/min thermal ramp from 30°C to 95°C with fluorescent detection at 330 and 350 nm. Data were analyzed with PR.ThermControl software v2.1.5 to determine the temperatures for T_onset and T_m. Figures 1M, S7, and S8K were made with GraphPad Prism v8.0.1.

Rumachik N.G., Malaker S.A., Poweleit N., Maynard L.H., Adams C.M., Leib R.D., Cirolia G., Thomas D., Stamnes S., Holt K., Sinn P., May A.P, & Paulk N.K. (2020). Methods Matter: Standard Production Platforms for Recombinant AAV Produce Chemically and Functionally Distinct Vectors. Molecular Therapy. Methods & Clinical Development, 18, 98-118.

+ 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?

Revolutionizing how scientists
search and build protocols!