J 815 cd spectrometer

Manufactured by Jasco

Sourced in Japan, United States, United Kingdom, Germany, Canada, Brazil

The J-815 CD spectrometer is a laboratory instrument designed to measure the circular dichroism (CD) spectrum of samples. It is capable of analyzing the interactions between light and optically active molecules, providing information about the structural and conformational properties of the sample. The J-815 CD spectrometer operates within a specified wavelength range and can be used to study a variety of biomolecules, such as proteins, nucleic acids, and small organic compounds.

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Lab products found in correlation

Spectra manager software, by Jasco (7 mentions) 1 mm high precision quartz cell, by Hellma (7 mentions) Spectramanager 2 analysis software, by Jasco (5 mentions) Apex 2 spectrometer, by Bruker (4 mentions) Peltier thermal controlled cuvette holder, by Jasco (4 mentions) Ptc 423s 15, by Jasco (4 mentions) Spectra manager version 2, by Jasco (4 mentions) V 650 spectrophotometer, by Jasco (4 mentions) P 2000 polarimeter, by Jasco (4 mentions) Zeba spin desalting column, by Thermo Fisher Scientific (2 mentions) Peltier device, by Jasco (2 mentions) P 1020 digital polarimeter, by Jasco (2 mentions) System 2000 ft ir spectrophotometer, by PerkinElmer (2 mentions) V 530 uv vis spectrophotometer, by Jasco (2 mentions) Ptc 423, by Jasco (2 mentions) Chirascan cd spectrometer, by Applied Photophysics (2 mentions) Cdf 426s 15 peltier temperature control system, by Jasco (2 mentions) Matlab cftool, by MathWorks (2 mentions) Ptc 423s, by Thermo Fisher Scientific (2 mentions) Isotemp 3016, by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

J-815-150S CD spectrometer (3 citations) Model J-815 CD Spectrometer (4 citations) J-815 CD (21 citations) Jasco-815 CD spectrometer (37 citations) J-815 spectrometer (192 citations) J-815 (339 citations) 815 spectrometer (19 citations) CD spectrometer (22 citations)

424 protocols using j 815 cd spectrometer

Protein Characterization by Spectroscopy

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The protease-treated and the heat-treated protein solutions were characterized using CD spectroscopy and UV-Vis spectrophotometry. The CD spectra were collected within 190 to 400 nm wavelength range with 100 nm/min scanning speed using a quartz cell cuvette of 10 mm path length and a JASCO J-815 CD spectrometer at room temperature. All the spectra were the average of three consecutive scans for each sample. The CD spectra were subjected to minimal smoothing (using ‘Spectra Manager’ software provided with the JASCO J-815 CD spectrometer) so that no alteration of the signal and/or loss of signal occurred. The UV-Vis spectra were acquired using Varian Cary 50 Bio UV-Vis spectrophotometer and a 1 cm cuvette at room temperature.

Kolay J., Bera S, & Mukhopadhyay R. (2021). How stable are the collagen and ferritin proteins for application in bioelectronics?. PLoS ONE, 16(1), e0246180.

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CD Spectroscopy of Enzyme Stability

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CD spectra were acquired on a JASCO J-815 CD spectrometer (Jasco, Tokyo, Japan) controlled by a CDF-426S/15 Peltier temperature control system using a quartz cuvette with a 1-cm path length. The enzyme was prepared in phosphate buffer (20 mM sodium phosphate, 150 mM NaCl, pH 7.5) at a final concentration of 8 µM. All spectra were obtained at 20 °C in the range 195–260 nm with a bandwidth of 2 nm and a response time of 4 s nm⁻¹. CD spectra were buffer subtracted and normalized to mean residue ellipticity. Thermal unfolding experiments were monitored at 220 nm in the temperature range 20–90 °C with a scan rate of 1 °C min⁻¹. The melting temperature was determined according to the sigmoidal-Boltzmann fitting of the CD denaturation curve.

dos Santos C.R., de Giuseppe P.O., de Souza F.H., Zanphorlin L.M., Domingues M.N., Pirolla R.A., Honorato R.V., Tonoli C.C., de Morais M.A., de Matos Martins V.P., Fonseca L.M., Büchli F., de Oliveira P.S., Gozzo F.C, & Murakami M.T. (2018). The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans. Biotechnology for Biofuels, 11, 223.

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Circular Dichroism Analysis of SAAP-148 Peptides

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Circular dichroism spectroscopy was performed at room temperature using a Jasco J-815 CD spectrometer with a 1 mm path-length cell and a bandwidth of 2.0 nm. SAAP-148 and SAAP-148-PEG₂₇ were prepared in 10 mm sodium phosphate (NaPi) buffer (pH 7.4) with a final peptide concentration of 0.2 mg/mL. Further analysis was performed by addition of 25% 2,2,2-trifluoroethanol (TFE; α-helix enhancer) or 1–10 mm sodium dodecyl sulfate (SDS; β-sheet enhancer or α-helix enhancer at non-micellar and micellar concentration, respectively). Spectra were recorded from 190 to 260 nm at an interval of 0.1 nm. Each spectrum was the average of five scans and blank subtraction. Secondary structure composition differences were calculated using the software CDNN 2.1 (developed by Applied Photophysics Ltd.).

van Gent M.E., Schonkeren-Ravensbergen B., Achkif A., Beentjes D., Dolezal N., van Meijgaarden K.E., Drijfhout J.W, & Nibbering P.H. (2023). C-Terminal PEGylation Improves SAAP-148 Peptide’s Immunomodulatory Activities. Journal of Innate Immunity, 15(1), 724-738.

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Comprehensive Optical Characterization Protocol

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UV–Vis absorption and PL spectroscopy were carried out using a Cary 8454 UV–Vis spectrophotometer and FluoroMax‐3 fluorescence spectrophotometer (Horiba), respectively. PL QYs were measured using the comparison approach using Rhodamine 6G in ethanol (PL QY = 95%) as a standard. Transmission electron microscopy (TEM) was performed using a JEOL 3100R05 electron microscope operating at a beam voltage of 300 kV. X‐ray photoelectron spectroscopy (XPS) was performed using a Kratos Axis Ultra XPS. Fourier‐transform infrared (FTIR) spectroscopy was carried out using JASCO (FT/IR‐4100) FTIR spectrometer. Nuclear magnetic resonance (NMR) spectroscopy was performed using Bruker Advance Neo 500 spectrometer. Circular dichroism (CD) spectroscopy was carried out using a J‐815 CD spectrometer (JASCO, Japan) operating under a N₂ flow of 5–8 l/min. Typical scanning parameters were as follows: scanning speed, 100 nm/min; data pitch, 1 nm; bandwidth, 1 nm, digital integration time, 2 sec; and one accumulation. The anisotropy factor (g‐factor) was calculated according to the equation g = CD/(32,980·Abs), where CD is the signal obtained from CD/DC channel (in mdeg) and Abs is the total absorbance. CD spectra were stopped at wavelengths where the hydrothermal voltage exceeded 400 V to avoid artifacts during acquisition.

Visheratina A., Hesami L., Wilson A.K., Baalbaki N., Noginova N., Noginov M.A, & Kotov N.A. (2022). Hydrothermal synthesis of chiral carbon dots. Chirality, 34(12), 1503-1514.

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Conformational Analysis of Ramosin Peptide

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The analysis of the conformation of the Ramosin peptide was performed through circular dichroism (CD). CD spectroscopy was carried out on a JASCO J-815 CD Spectrometer (JASCO Corp., Tokyo, Japan) in the far ultraviolet (UV) range (190–250 nm), using quartz cuvettes (0.1 cm path length). Each CD spectra of the synthetic peptide was recorded, averaging three scans in continuous scanning mode. Solvent blank was subtracted from each sample spectrum. Molar ellipticity was calculated for each spectra using 250 µL of 2 mM peptide in 30% (v/v) 2,2,2-trifluoroethanol (TFE), water, phosphate buffered saline (PBS) 2 mM pH = 7.4, sodium bicarbonate buffer 1 M pH = 8.5, and sodium acetate 3 M pH = 5. Resulting data were analyzed using Spectra Manager software (Version 2.0, JASCO Corp., Tokyo, Japan) [41 (link),42 (link)].

Medina L., Guzmán F., Álvarez C., Delgado J.P, & Carbonell-M B. (2022). Ramosin: The First Antibacterial Peptide Identified on Bolitoglossa ramosi Colombian Salamander. Pharmaceutics, 14(12), 2579.

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Circular Dichroism Spectroscopy of Proteins

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The freshly digested protein samples were diluted to 0.02 wt% using deionized water and loaded into a high-quality quartz cuvette with 1 mm optical path length. CD spectra were collected using a Jasco J-815 CD spectrometer with a wavelength ranging from 190–280 nm, bandwidth 2 nm, and scan speed 100 nm/min.

Xu D., Zhou J., Soon W.L., Kutzli I., Molière A., Diedrich S., Radiom M., Handschin S., Li B., Li L., Sturla S.J., Ewald C.Y, & Mezzenga R. (2023). Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment. Nature Communications, 14, 6806.

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Circular Dichroism Analysis of Protein Secondary Structure

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Secondary structure of ACE-MAP and ACE_BINDER was measured using the Jasco J-815 CD spectrometer with a PTC-423S single position Peltier temperature control system. Wavelength scans of ACE-MAP (10 µM) were performed from 195 to 250 nm at 1 nm step sizes. ACE_BINDER was first reconstituted in DMSO prior to dilution in PBS. SEC was used to remove remaining DMSO prior to CD. Temperature scans were performed from 25 ºC to 85 ºC at 1 ºC step sizes. The mean residue ellipticity (MRE) and melting temperature (T_m) – using 222 nm for ACE-MAP and 214 nm for ACE_BINDER – were calculated as described in previous studies [27] (link). The secondary structure content (α-helicity, β-content, and unordered structure) was predicted with CONTIN/LL software [58] (link), [59] (link), [60] (link).

Britton D., Punia K., Mahmoudinobar F., Tada T., Jiang X., Renfrew P.D., Bonneau R., Landau N.R., Kong X.P, & Montclare J.K. (2022). Engineered multivalent self-assembled binder protein against SARS-CoV-2 RBD. Biochemical Engineering Journal, 187, 108596.

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Circular Dichroism Spectroscopy of Proteins

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CD spectra were recorded in 1-mm quartz cuvettes on a J-815 CD spectrometer (Jasco). All data were collected from 200 to 260 nm at a scanning speed of 50 nm/min at 293 K. Three scans were averaged for each sample. All proteins were used at a concentration of 100 μm. The α-helical content was calculated from the value at 222 nm (30 (link)). Secondary structure contents were predicted using the K2D3 software (31 (link)).

Kuwabara N., Minami R., Yokota N., Matsumoto H., Senda T., Kawahara H, & Kato R. (2015). Structure of a BAG6 (Bcl-2-associated Athanogene 6)-Ubl4a (Ubiquitin-like Protein 4a) Complex Reveals a Novel Binding Interface That Functions in Tail-anchored Protein Biogenesis. The Journal of Biological Chemistry, 290(15), 9387-9398.

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Optical Characterization of Helical Nanostructures

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Purified spherical helix cluster was mixed with the Gold Enhancement reagent (Nanoprobes) with a volume ratio of 1:0.3 and incubated at room temperature for ~30 min.^{43 (link)} The circular dichroism and optical absorption of helical clusters were measured by a Jasco J-815 CD spectrometer.

Sun S., Yang S., Xin H.L., Nykypanchuk D., Liu M., Zhang H, & Gang O. (2020). Valence-programmable nanoparticle architectures. Nature Communications, 11, 2279.

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Spectroscopic Analysis of Iron-Bound ISCU

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Electronic absorption spectra in the UV-visible domain were acquired using a Secomam UVIKON XL spectrometer and CD spectra using a Jasco J-815 CD spectrometer. For experiments performed in other buffers, the apo-ISCU proteins in T2 buffer were buffer exchanged in buffer P (50 mM phosphate, 100 mM NaCl, pH 8.0), H7 (20 mM HEPES, 300 mM NaCl, pH 7.0) or H8 (20 mM HEPES, 300 mM NaCl, pH 8.0) by SEC on a NAP5 column. Then the proteins (5 μL, 2 mM) were mixed with 5 μL of ferrous ammonium sulfate (2 mM) prepared in water and the solution were completed to 100 μL with the corresponding buffer.
For experiments performed in Tris buffer at various pH, 5 μL of apo-ISCU proteins (2 mM) in T2 buffer were incubated with different ratios of buffer T2 and buffer T3 (20 mM Tris, 100 mM NaCl, pH 6.5). T2:T3 volume ratios of 45:45 μL, 15:75 μL and 8:82 μL were used to reach final pH of 7.7, 7.4 and 7.2. Then the protein samples were mixed with 5 μL of ferrous ammonium sulfate (2 mM) prepared in water.

Srour B., Gervason S., Hoock M.H., Monfort B., Want K., Larkem D., Trabelsi N., Landrot G., Zitolo A., Fonda E., Etienne E., Gerbaud G., Müller C.S., Oltmanns J., Gordon J.B., Yadav V., Kleczewska M., Jelen M., Toledano M., Dutkiewicz R., Goldberg D.P., Schünemann V., Guigliarelli B., Burlat B., Sizun C, & D’Autréaux B. (2022). Iron insertion at the assembly site of the ISCU scaffold protein is a conserved process initiating Fe-S cluster biosynthesis. Journal of the American Chemical Society, 144(38), 17496-17515.

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