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Ptc 423

Manufactured by Jasco
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Sourced in Japan, United States

The PTC-423S is a programmable thermal cycler designed for DNA amplification and other temperature-dependent applications. It features a compact design, intuitive interface, and temperature control capabilities for reliable and consistent results.

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Lab products found in correlation

J 810 spectropolarimeter, by Jasco (5 mentions) J 815 spectropolarimeter, by Jasco (4 mentions) J 810, by Jasco (4 mentions) J 1500 spectropolarimeter, by Jasco (2 mentions) J 815 cd spectrometer, by Jasco (2 mentions) J 715 cd spectrometer, by Jasco (1 mentions) Quartz cuvette, by Hellma (1 mentions) J 815 spectrometer, by Jasco (1 mentions) Ptc 423 peltier cell holder, by Jasco (1 mentions) J 815, by Jasco (1 mentions) J 715, by Jasco (1 mentions) J 815 cd spectropolarimeter, by Jasco (1 mentions) Sypro orange dye, by Merck Group (1 mentions) Step one real time pcr system, by Merck Group (1 mentions) 1 mm quartz cuvette, by Hellma (1 mentions)

Spelling variants of this product

PTC-423S/15 (16 citations) Model PTC-423S (5 citations) PTC-423S Peltier-type single position cell holder (3 citations) PTC 423S/15 Peltier temperature controller (3 citations) PTC-423S temperature controller (3 citations) PTC-423S/L (2 citations) PTC-423S/15 temperature (2 citations) PTC-423S temperature (2 citations) PTC-423 Peltier Cell Holder (2 citations)

25 protocols using ptc 423

1

CD Spectroscopy Analysis of Samples

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CD spectroscopy was performed
with a J-715 CD spectrometer (JASCO Corporation, Japan) using a Peltier
thermostated cell holder (PTC-423, JASCO Corporation) with a recirculating
cooler (JULABO F250, JASCO Corporation). Nitrogen flow (∼2.7
L/min) was led through the spectrometer and controlled with a nitrogen
flow monitor (Afriso Euro-Index). The samples were measured in double-distilled
water (Milli-Q H2O) at 1 mg/mL. The samples were measured
repeatedly (n = 3) in a quartz cuvette with d = 0.1 mm. Spectra were recorded at 25 °C from 300
to 180 nm using a data pitch, a bandwidth of 0.2 nm, and a scan speed
of 50 nm/min. The final spectra were produced by combining 10 individual
spectra and then expressed in molar ellipticity.
Duro-Castano A., Rodríguez-Arco L., Ruiz-Pérez L., De Pace C., Marchello G., Noble-Jesus C, & Battaglia G. (2021). One-Pot Synthesis of Oxidation-Sensitive Supramolecular Gels and Vesicles. Biomacromolecules, 22(12), 5052-5064.
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2

Circular Dichroism Analysis of D-QK Peptide

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Circular dichroism (CD) spectroscopy studies on the D-QK peptide were performed using a Jasco J-715 spectropolarimeter equipped with a PTC-423 Peltier temperature controller. CD spectra were recorded as average of three scans, at 20 °C, in the far-UV wavelength range 260–190 nm, using a scanning speed of 10 nm min−1, a band width of 1 nm, a data pitch of 0.1 nm, a response of 2 sec, and using a 0.1 cm path-length quartz cuvette (Hellma). CD spectra were recorded at 100 µM peptide concentration in filtered and degassed 5 mM potassium phosphate buffer, pH 7.0, and in filtered and degassed H2O containing an increasing concentration of the cosolvent trifluoroethanol (TFE) (Sigma-Aldrich) (0, 5%, 10%, 15%, 20%, 30%, 40% of TFE). Peptide concentration was determined by UV-spectroscopy, measuring the absorbance at 280 nm of the peptide solution and using the Lambert-Beer equation and the molar extinction coefficient of 8480 M−1 cm−1. All CD spectra have been smoothed and the buffer or solvent contribution has been subtracted using the Spectra Manager software. CD data are expressed as mean residue ellipticity [θ].
De Rosa L., Diana D., Capasso D., Stefania R., Di Stasi R., Fattorusso R, & D’Andrea L.D. (2022). Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide. Molecules, 27(20), 6982.
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3

Characterization of Molecular Structure

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UV-vis and electronic circular dichroism (ECD) spectra were measured on a JASCO J-815 spectrometer equipped with a JASCO Peltier cell holder PTC-423 to maintain the temperature at 20°C. A quartz photoelastic modulator set at l/4 retardation was used to modulate the handedness of the circular polarized light at 50 kHz. The CD spectrometer was purged with nitrogen during the recording of spectra. The UV absorption and ECD spectra were recorded simultaneously using the buffer as a reference.
Patra S., Claude J.B., Naubron J.V, & Wenger J. (2021). Fast interaction dynamics of G-quadruplex and RGG-rich peptides unveiled in zero-mode waveguides. Nucleic Acids Research, 49(21), 12348-12357.
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4

Protein Unfolding Monitored by Circular Dichroism

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Protein unfolding was monitored by circular dichroism in a J-810 spectropolarimeter (JASCO, Tokyo, Japan) equipped with a Jasco PTC-423 temperature controller. The sample was diluted to 1–2 μM in 20 mM Tris-HCl, pH 8.0 and denaturation curves recorded at a wavelength of 210 nm from 10 to 90 °C at a heating rate of 1 °C/min. The bandwidth used was 2 nm. Melting temperatures (TM) were calculated as the maxima of the first derivatives of the percentage of change of ellipticity at 210 nm versus temperature curves. For a clear depiction of the kinetic traces, data points were smoothed by the group reduction function implemented in OriginPro software. This function calculates new x and y values from the average of ten x-axis and ten y-axis points, respectively.
Morante K., Bellomio A., Viguera A.R., González-Mañas J.M., Tsumoto K, & Caaveiro J.M. (2019). The Isolation of New Pore-Forming Toxins from the Sea Anemone Actinia fragacea Provides Insights into the Mechanisms of Actinoporin Evolution. Toxins, 11(7), 401.
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5

Circular Dichroism Spectroscopy of Proteins

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CD measurements were performed with a Jasco J-1500 spectropolarimeter. Experiments were performed at 298 K using a Jasco PTC-423 Peltier cell holder connected to a Jasco PTC-423S Peltier controller. Far-UV CD spectra were collected using a cylindrical cell (121-0.20-40 from Hellma) with 0.2 mm optical path length using 50 µL of protein solution. Data were acquired at a scan speed of 20 nm/min and at least three scans were averaged. Proteins were used at a concentration of 50 µM, in a 0.5 mM Tris-HCl pH 7.0, 1 mM KCl buffer. For experiments with ferrous iron, the cuvette was filled and sealed under anaerobic atmosphere in a glove box; the compartment of the CD spectropolarimeter is anaerobic since it is constantly under nitrogen flow.
Doni D., Passerini L., Audran G., Marque S.R., Schulz M., Santos J., Costantini P., Bortolus M, & Carbonera D. (2020). Effects of Fe2+/Fe3+ Binding to Human Frataxin and Its D122Y Variant, as Revealed by Site-Directed Spin Labeling (SDSL) EPR Complemented by Fluorescence and Circular Dichroism Spectroscopies. International Journal of Molecular Sciences, 21(24), 9619.
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6

Secondary Structure Analysis of SsArd1

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CD experiments involved a Jasco J-810 spectropolarimeter (Jasco International, USA) with a Peltier effect temperature controller (Jasco PTC-423S). Secondary structure determination spectra of wild-type and mutated SsArd1 were examined with 30 μM protein in 20 mM phosphate buffer, pH 8.0, and 2 mM NaCl at 25°C. The spectra were measured in a 1-mm quartz cuvette at wavelength 195 to 260 nm. All samples were centrifuged at 10,000 g for 10 min before analysis. CD spectra for the SsArd1 structure at different temperatures were obtained by heating the sample from 25 to 95°C. The data collection parameters were scanned rate 50 nm/min, response time 1 s, sensitivity 100 mdeg, accumulation 3, heating rate 1°C/min and delay time for collection 60 s. The reversibility of the temperature effect was checked by cooling the sample to 25°C with the same parameters. Baseline subtraction, smoothing and data normalization involved use of SigmaPlot. The CD data are shown as mean residue ellipticity units (deg cm2 dmol−1).
Chang Y.Y, & Hsu C.H. (2015). Structural Basis for Substrate-specific Acetylation of Nα-acetyltransferase Ard1 from Sulfolobus solfataricus. Scientific Reports, 5, 8673.
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7

Circular Dichroism Spectroscopy of Biomolecules

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The circular dichroism (CD) measurements were done on a Jasco J-815 (JASCO Inc., Tokyo, Japan) spectropolarimeter equipped with a Peltier temperature control PTC-423-S. Samples were prepared at a concentration of 0.5 mg/mL in a 25 mM sodium phosphate buffer at pH 7.4 or KCl 25 mM at pH 7.4, as indicated. All acquisitions were taken in the spectral range of 190–260 nm at 25 °C, using a 0.5 mm quartz cuvette, with a scanning speed of 100 nm/min, a bandwidth of 2 nm, and a response time of 1 s.
Manieri T.M., Sensi S.L., Squitti R, & Cerchiaro G. (2021). Structural effects of stabilization and complexation of a zinc-deficient superoxide dismutase. Heliyon, 7(1), e06100.
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8

Circular Dichroism Analysis of Protein Constructs

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All circular
dichroism data were
collected in a Jasco 720 instrument with a Jasco model PTC-423S single-position
Peltier attachment controller using a 0.1 mm path length cuvette.
Data were collected on each construct at two concentrations (0.75
and 1.25 mg/mL). At each concentration, three spectra were recorded
and averaged at 10 °C intervals from 5 to 65 °C. The ellipticity
at 196 nm was also measured at 1 °C intervals from 5 to 65 °C
to compare the effect of temperature and concentration on β-turn
formation.
Lyons D.F., Le V., Kramer W.H., Bidwell GL I.I.I., Lewis E.A., Raucher D, & Correia J.J. (2014). Effect of Basic Cell-Penetrating Peptides on the Structural, Thermodynamic, and Hydrodynamic Properties of a Novel Drug Delivery Vector, ELP[V5G3A2-150]. Biochemistry, 53(6), 1081-1091.
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9

CD Spectroscopy of Bri2-23 Peptide Interactions

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CD spectra were recorded using a Jasco J-815 spectropolarimeter and the temperature was controlled with a PTC-423S temperature controller. A quartz cell with 1 cm optical path was used. The spectra range was 190-260 nm with a resolution of 0.1 nm and a bandwidth of 1 nm. A scan speed of 20 nm min À1 with 1 s response time was employed. Baseline spectra were subtracted from each spectrum and data were smoothed using the Savitzky-Golay method. Data were processed using Origin 7.0 spread sheet/graph package. The direct CD measurements (y, in millidegrees) were converted to mean residue molar ellipticity, using the relationship mean residue De = y/(33 000  c  l  number of residue). 10 mM solution of apo and metal (Ag(I) and Hg(II)) bound Bri2-23 either in phosphate buffer (50 mM) and at acidic pH (B3.0) were analyzed.
Luczkowski M., De Ricco R., Stachura M., Potocki S., Hemmingsen L, & Valensin D. (2015). Metal ion mediated transition from random coil to β-sheet and aggregation of Bri2-23, a natural inhibitor of Aβ aggregation. Metallomics : integrated biometal science, 7(3).
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10

Circular Dichroism Analysis of Oligonucleotides

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CD spectra and CD melting curves of oligonucleotides were recorded on a Jasco J-715 spectropolarimeter equipped with a Jasco PTC-423S Peltier temperature controller. CD spectra were recorded in the wavelength range 230–360 nm at 20°C, with a scan rate of 100 nm/min, a response time of 1 s and a bandwidth of 1 nm. All the spectra were averaged over 3 scans. Buffer baseline was subtracted from each spectrum. The DNA concentration was 10 μM (as single strand) and ligand stock solution was 1.5 mM in DMSO. DNA/ligand mixtures were obtained by adding 4 molar equiv. of ligands (40 μ M). CD melting were performed in the temperature range 20–100°C, at the heating rate of 1°C/min by following changes of the CD signal at the wavelengths of maximum variations upon oligonucleotide folding. The melting temperatures were determined from fit of melting curves using two state transition model implemented in Origin 8.0 program. Each melting experiment was performed at least three times.
Amato J., Iaccarino N., Pagano B., Morigi R., Locatelli A., Leoni A., Rambaldi M., Zizza P., Biroccio A., Novellino E, & Randazzo A. (2014). Bis-indole derivatives with antitumor activity turn out to be specific ligands of human telomeric G-quadruplex. Frontiers in Chemistry, 2, 54.
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