J 820

Manufactured by Jasco

Sourced in Japan

The J-820 is a spectrophotometer designed for accurate and reliable analysis of samples. It is capable of measuring the absorption or transmission of light across a wide range of wavelengths, providing precise data on the optical properties of materials.

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Lab products found in correlation

Milli q reference, by Merck Group (2 mentions) Elix uv, by Merck Group (2 mentions) R axis 4, by Rigaku (2 mentions) Ptc 423l, by Jasco (2 mentions) Ft 620, by Jasco (2 mentions) Lc 20at, by Shimadzu (2 mentions) Spectra manager, by Jasco (1 mentions) Bioshaker br 23fp, by TAITEC (1 mentions) Sybr gold, by Thermo Fisher Scientific (1 mentions) Ultra low range dna ladder, by Thermo Fisher Scientific (1 mentions) Vk x3000, by Keyence (1 mentions) Dsc 50, by Shimadzu (1 mentions) Uv 3600, by Shimadzu (1 mentions) Hi qras gel n, by Kanto Chemical (1 mentions) Novex ph 3 10, by Thermo Fisher Scientific (1 mentions) Eps 301, by GE Healthcare (1 mentions) Eps 601, by GE Healthcare (1 mentions) Ptc 423l peltier temperature controller, by Jasco (1 mentions) Uv 1800, by Shimadzu (1 mentions) Supersep ace, by Fujifilm (1 mentions)

64 protocols using j 820

Circular Dichroism Characterization of CTD Peptides

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The nonacetyl and acetyl CTD fragments were dissolved in Milli‐Q water at 200 μM. The peptide solutions were diluted to 40 μM with the desired concentration of trifluoroethanol (TFE) for circular dichroism (CD) measurements. To detect the helix propensity, we varied TFE concentrations of 0–50%. It is noteworthy that the TFE concentrations in this article are volume per volume percentages. The peptide solutions also contained 25 mM sodium phosphate (pH 7.0 without TFE) and 0.1 M sodium chloride. Because pH is 7.0, the histidine state is neutral. Consequently, the fragments treated in this CD measurement are also designated as NonAc and Ac.
We performed far‐UV CD measurements of the peptide solutions. Far‐UV CD spectra were recorded on a spectropolarimeter (JASCO J‐820; Jasco Corp., Japan) at 25°C using a quartz cuvette with 1‐mm path length. The spectra were expressed as the mean residue ellipticity and [θ] (deg cm² dmol⁻¹). All spectra were estimated iteratively 16 times. Furthermore, this procedure was repeated three times to compute the average and standard deviation of the spectrum.

Iida S., Mashimo T., Kurosawa T., Hojo H., Muta H., Goto Y., Fukunishi Y., Nakamura H, & Higo J. (2016). Variation of free‐energy landscape of the p53 C‐terminal domain induced by acetylation: Enhanced conformational sampling. Journal of Computational Chemistry, 37(31), 2687-2700.

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CD Spectroscopy of Peptide Assemblies

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CD spectra of the peptide assemblies in aqueous solutions were recorded under the nitrogen atmosphere using a spectrophotometer JASCO J-820 (Jasco, Japan). A quartz cuvette with 0.5 mm path length was used as a sample container. Continuous scanning mode is applied. And each sample is scanned three times to obtain an averaged spectrum.

Hu X., Roy S.R., Jin C., Li G., Zhang Q., Asano N., Asahina S., Kajiwara T., Takahara A., Feng B., Aoki K., Xu C, & Zhang Y. (2022). Control cell migration by engineering integrin ligand assembly. Nature Communications, 13, 5002.

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Comparative Structural Analysis of Recombinant b5Rs

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The secondary structure of the recombinant proteins was spectroscopically evaluated by CD
using a spectropolarimeter (Jasco J-820, JASCO Ltd., Tokyo, Japan). Far-UV (200–250 nm)
and near-UV (250–300 nm) CD spectra of wild-type and Ile194Leu b5Rs were obtained at 1-nm
intervals using protein concentrations of 0.11 and 0.13 mg/ml, respectively, in PBS. The
CD spectra were measured at 25°C. The magnitude of the CD spectra was expressed as molar
ellipticity [θ], deg·cm²/dmol, based on the molecular weight of b5R (32,000
Da).
The thermostability and unfolding of the wild-type and Ile194Leu b5Rs were determined
according to the changes in the CD signal at 222 nm using temperature scans ranging from
10 to 80°C, increasing at the rate of 1°C/min. The wild-type and Ile194Leu b5Rs were
suspended in PBS at protein concentrations of 0.27 and 0.23 mg/ml, respectively. The
fraction at which 50% of the total protein was folded and unfolded was determined as the
Tm (melting temperature midpoint of the transition) value, and was
calculated for both wild-type and mutant b5Rs using the JWTDA-488 software (JASCO
Ltd.).

OTSUKA-YAMASAKI Y., INANAMI O., SHINO H., SATO R, & YAMASAKI M. (2020). Characterization of a novel nicotinamide adenine dinucleotide-cytochrome b5 reductase mutation associated with canine hereditary methemoglobinemia. The Journal of Veterinary Medical Science, 83(2), 315-321.

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Characterization of Amyloid Fibrils by CD

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The CD spectra were measured using a CD spectrometer (JASCO Corp., J-820). The far- and near-UV CD spectra were acquired at wavelengths of 200–250 nm and 250–320 nm using quartz cells with light paths of 1 and 10 mm (JASCO Corp.), respectively. Thermal denaturation curves were obtained at wavelengths of 230 and 293.5 nm in the far- and near-UV regions, respectively, with a temperature change rate of 1 °C/min. The CD spectrum data were collected using Spectra Manager (Version 1.55.00, JASCO Corp.).
Regarding the amyloid fibrils, the sample solutions after HANABI assay had their β2m concentration adjusted to 0.15 mg/mL by dilution with deionized water. The 170-μL and 2-mL solutions were injected into a quartz cell with light paths of 1 mm and 10 mm, respectively.

Nakajima K., Yamaguchi K., Noji M., Aguirre C., Ikenaka K., Mochizuki H., Zhou L., Ogi H., Ito T., Narita I., Gejyo F., Naiki H., Yamamoto S, & Goto Y. (2022). Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis. Nature Communications, 13, 5689.

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Recombinant PrP Structural Analysis

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The mouse recombinant PrP was dialyzed in 5 mM of Tris–HCl (pH 7.5), treated with HFIP at room temperature for 3 h at the concentration shown in the figure, then CD measurement (J-820, JASCO Corporation, Tokyo, Japan) was performed. Before the CD measurement, Aβ (1–40) was diluted in PBS, followed by shaking at 250 rpm (TAITEC BioShaker BR-23FP), at 37 °C for 12 h.

Shimizu T., Nogami E., Ito Y., Morikawa K., Nagane M., Yamashita T., Ogawa T., Kametani F., Yagi H, & Hachiya N. (2021). Volatile Anesthetic Sevoflurane Precursor 1,1,1,3,3,3-Hexafluoro-2-Propanol (HFIP) Exerts an Anti-Prion Activity in Prion-Infected Culture Cells. Neurochemical Research, 46(8), 2056-2065.

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Circular Dichroism Spectroscopy of Proteins

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Circular dichroism (CD) spectra were obtained using a spectropolarimeter (J-820; Jasco Corp.). The sample concentration was 0.2 µM in PBS. Quartz cuvettes with 10-mm thickness were used for measurements of 200−250 nm.

Hosaka H., Haruki R., Yamada K., Böttcher C, & Komatsu T. (2014). Hemoglobin–Albumin Cluster Incorporating a Pt Nanoparticle: Artificial O2 Carrier with Antioxidant Activities. PLoS ONE, 9(10), e110541.

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Conformational Analysis of Proteins

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The structure of DNA/RNA was confirmed by CD spectrum analysis using 1 μM RNA in the buffer used for the phase separation assay with or without monovalent salts at 25 °C using a CD spectrometer (Jasco J-820) as described previously (8 (link)). For conformational analysis of wild-type and mutant FUS proteins (0.5 mg/ml), the purified protein samples were diluted in PBS (phosphate-buffered saline) to make 0.2 μM solution and then subjected to CD analysis in the presence or absence of 0.2 μM RNAs (Table S1). Under the adjusted same conditions, TDP-43 (0.2 μM) was analyzed as a control.

Ishiguro A., Lu J., Ozawa D., Nagai Y, & Ishihama A. (2021). ALS-linked FUS mutations dysregulate G-quadruplex-dependent liquid–liquid phase separation and liquid-to-solid transition. The Journal of Biological Chemistry, 297(5), 101284.

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Aβ β-sheet Structural Analysis

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To evaluate the formation of the β-sheet structures derived from Aβ, CD spectral measurements were performed using a J-820 (JASCO, Tokyo, Japan). Before measurement, the solutions of every sample were exchanged with a 10 mM sodium phosphate buffer using Amicon ultra 0.5 mL, and 3 kDa (Merck Millipore, Darmstadt, Germany) to remove DMSO. Each spectrum of EGCG- or DA-treated Aβ samples was subtracted from the corresponding solvents without Aβ. Thermal stability was performed from 20–100 °C by increasing the temperature by 2 °C/min.

Kaku T., Tsukakoshi K, & Ikebukuro K. (2021). Cytotoxic Aβ Protofilaments Are Generated in the Process of Aβ Fibril Disaggregation. International Journal of Molecular Sciences, 22(23), 12780.

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Circular Dichroism Analysis of Zein Protein Structures

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The secondary structures of the zein and zein–CA solutions were analyzed using circular dichroism (J-820, Jasco, Japan), which covered a scanning range of 190–260 nm. The baseline was 85% (v/v) ethanol. We used the following equation (Tiwari, Ali, Ishrat, & Arfin, 2021 (link)) to express CD results based on residue ellipticity (MRE):

{M R E}_{208} = \frac{o b s e r v e d C D (m i l l i d e g r e e)}{C_{p} n l \times 10}

In this equation, C_p is the molar concentration of the protein, n is the number of amino acid residues in zein (in this case 266), and L (0.1 cm) is the path length. The calculation equation for the α-helix content of the sample was as follows (Tiwari, Ali, Ishrat, & Arfin, 2021 (link)):

α - h e l i x (%) = - \frac{[{MRE}_{208} - 4000]}{33000 - 4000} \times 100

Wang X., Li X., Xue J., Zhang H., Wang F, & Liu J. (2022). Mechanistic understanding of the effect of zein–chlorogenic acid interaction on the properties of electrospun nanofiber films. Food Chemistry: X, 16, 100454.

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Circular Dichroism Spectroscopy of HSA

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CD spectra are measured on a JASCO J-820 automatic spectropolarimeter (JASCO, Tokyo, Japan) using a 0.1 cm cell. The buffer solution is used as a blank and automatically subtracted from the samples during scanning. Data are recorded from 200 to 250 nm with a scan speed of 100 nm·min⁻¹. The concentration of HSA is maintained at 1.5 × 10⁻⁶mol L⁻¹. The measurements are repeated three times.

Hou H., Qu X., Li Y., Kong Y., Jia B., Yao X, & Jiang B. (2015). Binding of Citreoviridin to Human Serum Albumin: Multispectroscopic and Molecular Docking. BioMed Research International, 2015, 162391.

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