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High sensitivity capillaries

Manufactured by NanoTemper
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High-sensitivity capillaries are precision-engineered glass tubes designed for use with NanoTemper's instrumentation. They provide a controlled environment for conducting sensitive biophysical measurements. The capillaries are optimized to enhance the detection and analysis of molecular interactions and transitions.

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Lab products found in correlation

Prometheus nt 48, by NanoTemper (6 mentions) Prometheus panta, by NanoTemper (3 mentions) Prometheus panta device, by NanoTemper (1 mentions) Prometheus nt 48 nanodsf, by NanoTemper (1 mentions)

Spelling variants of this product

NanoDSF grade high-sensitivity glass capillaries (6 citations) Prometheus NT.48 high-sensitivity capillaries (4 citations) Prometheus NT.48 Series nanoDSF Grade High Sensitivity Capillaries (3 citations) Prometheus High Sensitivity Capillaries (2 citations) Prometheus Series High Sensitivity Capillaries (1 citations)

12 protocols using high sensitivity capillaries

1

Protein Size Characterization by DLS

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Dynamic Light Scattering was used for isothermal particle sizing. Briefly, proteins were diluted to a final concentration of 2.5 µM and loaded to High Sensitivity capillaries (NanoTemper Technologies GmbH, Munich, Germany). Measurements were carried out at 20 °C in triplicates of 10 acquisitions each with a Prometheus Panta device (NanoTemper Technologies GmbH, Munich, Germany). The hydrodynamic radius of the particles in solvated state and the polydispersity index (PDI) of the samples were determined with the associated software.
Hauser A., Carnell G., Held K., Sulbaran G., Tischbierek N., Rogers L., Pollakis G., Tonks P., Hoelscher M., Ding S., Sanders R.W., Geldmacher C., Sattentau Q., Weissenhorn W., Heeney J.L., Peterhoff D, & Wagner R. (2021). Stepwise Conformational Stabilization of a HIV-1 Clade C Consensus Envelope Trimer Immunogen Impacts the Profile of Vaccine-Induced Antibody Responses. Vaccines, 9(7), 750.
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2

Dynamic Light Scattering of Ola1p

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DLS measurements were done using the Prometheus Panta (Nanotemper). For DLS measurements with good signal-to-noise, 10 μM or 0.5 mg/ml Ola1p in 20 mM PIPES pH 7.0 buffer with a final salt concentration of 100 mM KCl and 1 mM TCEP was used. Samples in the presence and absence of 2 mM ATP with 2 mM MgCl2 were loaded in high-sensitivity capillaries (Nanotemper) and heated with a 0.3 °C/min temperature ramp from 20 °C to 70 °C with a 2 s DLS integration time. The cumulative radius and polydispersity index (PDI) values were determined using the Prometheus Panta software (Nanotemper).
Dannenmaier S., Desroches Altamirano C., Schüler L., Zhang Y., Hummel J., Milanov M., Oeljeklaus S., Koch H.G., Rospert S., Alberti S, & Warscheid B. (2021). Quantitative proteomics identifies the universally conserved ATPase Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 297(5), 101050.
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3

Unfolding Transitions of mGFP-CAPRIN1 Variants

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mGFP-CAPRIN1 (WT or P512L) was diluted to a final protein concentration of 5 µM in 50 mM Tris/KOH pH 7.5 and 75 mM KCl. Unfolding transitions were recorded with a Prometheus Panta (Nanotemper) in high sensitivity capillaries (Nanotemper) at 0.3 °C min−1. Data analysis and plotting were with the R/RStudio software package.
Delle Vedove A., Natarajan J., Zanni G., Eckenweiler M., Muiños-Bühl A., Storbeck M., Guillén Boixet J., Barresi S., Pizzi S., Hölker I., Körber F., Franzmann T.M., Bertini E.S., Kirschner J., Alberti S., Tartaglia M, & Wirth B. (2022). CAPRIN1P512L causes aberrant protein aggregation and associates with early-onset ataxia. Cellular and Molecular Life Sciences, 79(10), 526.
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4

Nano-DSF Thermal Stability Profiling

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For nano-DSF measurements using the Prometheus NT.48 (Nanotemper, Munich), proteins were diluted to varying concentrations in 20 mM PIPES/KOH buffer pH 6.8 or pH 7.5 to a final concentration of 200 mM KCl and in the presence of 1 mM TCEP. Samples were heated in high sensitivity capillaries (Nanotemper, Munich) with 1°C increments per min from 20°C to 95°C. NanoDSF was also used to measure light scattering.
Iserman C., Desroches Altamirano C., Jegers C., Friedrich U., Zarin T., Fritsch A.W., Mittasch M., Domingues A., Hersemann L., Jahnel M., Richter D., Guenther U.P., Hentze M.W., Moses A.M., Hyman A.A., Kramer G., Kreysing M., Franzmann T.M, & Alberti S. (2020). Condensation of Ded1p Promotes a Translational Switch from Housekeeping to Stress Protein Production. Cell, 181(4), 818-831.e19.
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5

Thermal Stability Analysis of Spike and RBD

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NanoDSF was performed on a Prometheus NT.48 instrument (NanoTemper Technologies GmbH). Protein samples were centrifuged for 15 min before preparation. The final reaction mixture contained 4 μg of either Spike or RBD proteins diluted in PBS pH 7.4. High sensitivity capillaries (NanoTemper Technologies) were filled with 10 µl of sample and placed on the sample holder. A temperature gradient of 1°C/min was applied from 15°C to 95°C and the intrinsic protein fluorescence at 330 and 350 nm was recorded. Data were analysed using either the value of fluorescence at 330 nm (for Spike protein) or the derived ratio 350/330 value (for RBD protein). All samples were tested in duplicates.
Castro R., Nobre L.S., Eleutério R.P., Thomaz M., Pires A., Monteiro S.M., Mendes S., Gomes R.A., Clemente J.J., Sousa M.F., Pinto F., Silva A.C., Freitas M.C., Lemos A.R., Akpogheneta O., Kosack L., Bergman M., Duarte N., Matoso P., Costa J., Bandeiras T.M., Gomes‐Alves P., Gonçalves C.P., Demengeot J, & Alves P.M. (2021). Production of high‐quality SARS‐CoV‐2 antigens: Impact of bioprocess and storage on glycosylation, biophysical attributes, and ELISA serologic tests performance. Biotechnology and Bioengineering, 118(6), 2202-2219.
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6

Thermal Stability Analysis of Ola1p

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NanoDSF coupled to scattering measurements were done with the Prometheus NT.48 (Nanotemper). Ola1p was diluted to the indicated concentrations in 20 mM PIPES pH 7.0 buffer with a final concentration of 100 mM KCl and 1 mM TCEP. Samples were loaded in high-sensitivity capillaries (Nanotemper) and heated with a 0.5 °C/min temperature ramp from 20 °C to 70 °C.
Dannenmaier S., Desroches Altamirano C., Schüler L., Zhang Y., Hummel J., Milanov M., Oeljeklaus S., Koch H.G., Rospert S., Alberti S, & Warscheid B. (2021). Quantitative proteomics identifies the universally conserved ATPase Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 297(5), 101050.
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7

Protein Thermal Unfolding Profiling by DSF

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Prometheus NT.48 was used to measure the thermal unfolding profiles of proteins by differential scanning fluorimetry experiments (Prometheus NT.48, NanoTemper, Munich, Germany). All samples were used at a final concentration of 10 µM and loaded into high-sensitivity capillaries (Nanotemper, Munich, Germany). The protein unfolding process was subjected to a thermal ramp (20–95 °C, 1 °C/min). Data analysis involved using Prometheus PR ThermControl software (NT. 48, NanoTemper, Munich, Germany). The Tm value was determined by fitting the tryptophan 350/330 nm fluorescence emission ratio using a polynomial function in which the maximum slope is indicated by the peak of its first derivative.
Aubrey N., Gouilleux-Gruart V., Dhommée C., Mariot J., Boursin F., Albrecht N., Bergua C., Croix C., Gilotin M., Haudebourg E., Horiot C., Matthias L., Mouline C., Lajoie L., Munos A., Ferry G., Viaud-Massuard M.C., Thibault G, & Velge-Roussel F. (2022). Anticalin N- or C-Terminal on a Monoclonal Antibody Affects Both Production and In Vitro Functionality. Antibodies, 11(3), 54.
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8

Thermal Stability Analysis of Proteins

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The samples with a concentration of 0.1 mg/mL were filled in high sensitivity capillaries (NanoTemper Technologies) and sealed. The capillaries were placed in a Prometheus NT.48 (NanoTemper Technologies) and a temperature ramp of 1 °C/min was applied, while the intrinsic protein fluorescence intensity at 350 nm was measured after excitation at 280 nm. The PR. ThermControl V2.1 software was used to determine the apparent melting temperatures from the fluorescence intensity signal at 350 nm.
Svilenov H.L., Sacherl J., Protzer U., Zacharias M, & Buchner J. (2021). Mechanistic principles of an ultra-long bovine CDR reveal strategies for antibody design. Nature Communications, 12, 6737.
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9

Thermal Unfolding of Protein Trimers

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Thermostability of the trimers was characterized by thermal unfolding with a Prometheus NT.48 nanoDSF (NanoTemper Technologies GmbH, Munich, Germany). Proteins were diluted to a final concentration of 0.05 mg/mL. After loading the samples to High Sensitivity capillaries (NanoTemper Technologies GmbH, Munich Germany), intrinsic fluorescence was measured at a ramp rate of 1 °C/min with an excitation power of 30%. Protein unfolding was monitored by the changes in fluorescence emission at 350 and 330 nm. The thermal unfolding midpoint (Tm) of the proteins was determined with Prometheus NT software.
Hauser A., Carnell G., Held K., Sulbaran G., Tischbierek N., Rogers L., Pollakis G., Tonks P., Hoelscher M., Ding S., Sanders R.W., Geldmacher C., Sattentau Q., Weissenhorn W., Heeney J.L., Peterhoff D, & Wagner R. (2021). Stepwise Conformational Stabilization of a HIV-1 Clade C Consensus Envelope Trimer Immunogen Impacts the Profile of Vaccine-Induced Antibody Responses. Vaccines, 9(7), 750.
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10

Thermal Unfolding of BG505-SOSIP

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Thermal unfolding of BG505-SOSIP was determined with a heating ramp of 1°C/min and 20% sensitivity setting using high-sensitivity capillaries (NanoTemper Technologies, Munich, Germany; Cat# PR-C006). BG505-SOSIP was diluted to 700 nM in selected FORMOscreen ® buffers (2bind, Regensburg, Germany, Cat# 2BBT-001).
Popp C., Schramm P., Wagner R., Peterhoff D., Battle C., Kleusch C., & Plach M.G. (2020). Multi-parameter formulation development for an HIV-vaccine protein with direct validation of epitope binding integrity and stoichiometry.
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