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Pfd 425s peltier unit

Manufactured by Jasco
Sourced in Japan

The PFD-425S Peltier-unit is a compact and efficient thermoelectric cooling device. It utilizes the Peltier effect to actively control the temperature of attached components or samples. The device provides precise temperature regulation and can be used for a variety of laboratory and scientific applications.

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4 protocols using pfd 425s peltier unit

1

Far-UV CD Spectroscopy of Amyloid-Beta

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Far-UV CD spectra of proteins and peptides in soluble and insoluble states were measured with a J-820 spectropolarimeter (Jasco, Japan) using a cell with a light path of 1 mm at each condition. Individual Aβ42 solutions were prepared at 10 μM for CD measurements. The CD signals between 195 and 250 nm were expressed as mean residue ellipticity [θ] (deg cm2 dmol–1). Temperature regulation was carried out using a PFD-425S Peltier-unit (Jasco, Japan).
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2

Far-UV CD Spectroscopy of Amyloid-β Peptides

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Far-UV CD spectra of proteins and peptides in soluble and insoluble states were measured with a J-820 spectropolarimeter (Jasco, Japan) using a cell with a light path of 1 mm at each condition. Individual Aβ42 solutions were prepared at 10 μM for CD measurements. The CD signals between 195 and 250 nm were expressed as mean residue ellipticity [θ] (deg cm2 dmol-1). Temperature regulation was carried out using a PFD-425S Peltier-unit (Jasco, Japan).
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3

Far-UV CD Spectroscopy of Amyloid-Beta

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Far-UV CD spectra of proteins and peptides in soluble and insoluble states were measured with a J-820 spectropolarimeter (Jasco, Japan) using a cell with a light path of 1 mm at each condition. Individual Aβ42 solutions were prepared at 10 μM for CD measurements. The CD signals between 195 and 250 nm were expressed as mean residue ellipticity [θ] (deg cm2 dmol−1). Temperature regulation was carried out using a PFD-425S Peltier-unit (Jasco, Japan).
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4

Circular Dichroism Spectroscopy Protocol

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CD spectra were recorded using a Jasco J-710 spectropolarimeter equipped with a PFD-425S peltier unit (Jasco, Easton, MD) and employed a 1-mm path-length quartz cuvette. Samples were equilibrated at each temperature for 10 min. Spectra were collected with a resolution of 0.5 nm, a scan rate of 20 nm/min, and were the average of eight scans. Reported spectra were baseline corrected for solvent and buffer contributions.
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