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Cary 670 ftir spectrometer

Manufactured by Agilent Technologies
Sourced in United States

The Cary 670 FTIR spectrometer is a laboratory instrument designed for infrared spectroscopy analysis. It is capable of measuring the absorption or transmission of infrared radiation by a sample, providing information about the chemical composition and molecular structure of the analyzed material.

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12 protocols using cary 670 ftir spectrometer

1

Characterization of Organic Compounds

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All solvents used were of reagent grade. SLS (Sigma-Aldrich, St. Louis, MO, USA, product of Spain,) and aspirin (Sigma-Aldrich, St. Louis, MO, USA, product of Spain) were used with no further purification. Melting points were measured in open tubes with a Stuart Scientific apparatus and were uncorrected. IR spectra in the region of 4000–370 cm−1 were obtained using a Cary 670 FTIR spectrometer (Agilent Technologies Santa Clara, CA, USA). The 1H-NMR spectra were recorded on a Bruker AC 400 MHz FT-NMR instrument in a DMSO-d6 solution (Bruker GmbH & Co. 28359 Bremen, Germany). A UV-1600 PC series spectrophotometer of VWR international GmbH, Darmstadt, Germany, was used to obtain electronic absorption spectra.
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2

Molecular Characterization of RB Xenograft Tumors

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The FPA-FTIR study of the RB xenograft tumor samples was performed to identify the difference between the samples. FPA-FTIR micro-spectroscopic images were recorded using a Cary 620 FTIR microscope using cooled liquid-N2 environment with 128 × 128 element FPA detector objective lens, 15 × (0.62 NA) attached with FTIR spectrometer (Cary 670 FTIR spectrometer, Agilent Technologies). The FTIR Spectra were collected in a transmission mode in the spectral range between 3800-900 cm−1. A single FTIR image was acquired in an area of 700 × 700 cm2. A single FTIR spectral image contain the array of 64 × 64 spectra obtained from binning of the signal captured on detectors from each square of 4 on FPA array consist of 128 × 128 elements. A resultant single spectrum of sample collected in FTIR image acquired on ca. 10.9 × 10.9 mm2 revealed the molecular information about the sample functional group. From each tumor sample 5 FTIR spectral images were obtained with a resolution of 4-cm−1 with 128 co-added scans, Blackman-Harris 3-Term apodization, Power-Spectrum phase correction and a zero-filling factor of 2 using Resolutions Pro software package (Agilent Technologies). Before each sample measurement, background measurements were performed using a clean surface of the substrate with the same acquisition parameters17 (link).
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3

FTIR Analysis of Amino Acids

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FTIR experiments were carried out on an Agilent Cary 670 FTIR spectrometer with a N2(l)-cooled MCT detector. Spectra were recorded at 2 cm−1 resolution. Aliquots of 10 μL were placed between CaF2 windows with a 25 μm Teflon spacer. The instrument was purged for 30 min with N2 prior to data acquisition. The transmission spectrum from the buffer system was used as a reference and subtracted in order to determine the absorption spectrum of the of amino acid solutions.
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4

Synthesis and Characterization of Polymeric Lenses

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Dimethylsulfoxide (DMSO, Riedel-de Haen, Seelze, Germany) was used without any further purification. Silver nitrate (AgNO3,) was purchased from Degussa (Berlin, Germany). For lens preparation, 2-hydroxyethyl-methacrylate (pHEMA), ethylene-glycole-dimethacrylate (EGDMA, MERCK, Germany), diphenyl-(2,4,6-trimethylbenzoyl)-phosphine oxide (TPO 97%, Sigma-Aldrich, Steinheim, Germany) as well as sodium chloride (NaCl, MERCK) and hydrochloric acid (HCl 37%, MERCK) were used. Tryptone tryptophan medium, beef extract powder, peptone bacteriological and soy peptone were purchased from Biolife. Agar (Louis, MO, USA, product of Spain) and yeast extracts were purchased from Fluka Analytical (Switzerland). D(+)-glucose and di-potassium hydrogen phosphate trihydrate were purchased from Merck. Melting points were measured in open tubes with a Stuart Scientific apparatus and were uncorrected. A UV-1600 PC series spectrophotometer of VWR was used to obtain electronic absorption spectra. ATR-FT-IR spectra in the region of 4000–370 cm−1 were obtained with a Cary 670 FTIR spectrometer (Agilent Technologies Inc., Santa Clara, CA, USA). XRF measurement was carried out with Rigaku NEX QC EDXRF analyzer, (Austin, TX, USA).
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5

Characterization of CN Stretch in Y96CNF

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FT IR spectra were acquired as previously described on an Agilent Cary 670 FT IR spectrometer and a N2(l)-cooled MCT detector.29 (link) For characterization of the CN stretch of Y96CNF, a 4500 ± 500 nm bandpass filter was placed in the beam path after the sample. The instrument was purged with dry N2(g) for 40 min before data were collected. Background transmission spectra were collected with WT P450cam at the same concentration that was used for the samples (0.5–2 mM) in the same buffer (100 mM potassium phosphate, 50 mM KCl, and 20% glycerol). Additional details are provided in the Supporting Information. All spectra shown are representative of at least three independent trials.
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6

Characterization of Human iNOS Proteins

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Expression and purification of the human iNOS proteins were performed as described.19 (link),26 (link) Each protein sample was loaded between two CaF2 windows separated by a 76 μm spacer. Visible spectra (Agilent Cary 300 Spectrometer) and FT IR spectra (Agilent Cary 670 FT-IR spectrometer) of all samples were recorded to ensure binding of CO. Details regarding the procedure of protein identification by mass spectrometry, Fe(II)–CO sample preparation, FT IR spectral acquisition, and subsequent processing are provided in the Supporting Information. 2D IR spectroscopy was conducted in the traditional BOXCARS geometry as previously described; see the Supporting Information for a complete description.27 -29 (link) The center line slope (CLS) analysis of the Tw-dependent 2D IR spectra along with fitting to the linear FT IR spectra was used to determine FFCFs parameters.30 (link),31 (link) Experiments were performed in triplicate with independently prepared samples, except for the full-length protein, for which we were only able to obtain duplicate data.
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7

FTIR Spectroscopy of Cyano-containing Compounds

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FT IR spectra were acquired using an Agilent Cary 670 FT IR spectrometer with a liquid N2-cooled MCT detector. Absorption spectra were generated from transmission spectra of CNSePhe, CNPhe, or cyano-alanine in H2O, DMSO and/or 65 : 35 methanol : H2O and reference transmission spectra of the pure solvents. A slowly varying baseline was removed by subtraction of a polynomial fit of the background from the spectra.
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8

FTIR Microscopy of Cell Samples

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All spectroscopic data was collected using an Agilent Cary 670 FTIR Spectrometer coupled to an Agilent Cary 620 FTIR Microscope (Agilent Technologies, Santa Clara, CA, USA) equipped with a liquid-N2 cooled detector. The microscope stage is enclosed with a custom-built chamber to displace the atmosphere with a nitrogen stream. A 7 × 7 tile mosaic was collected with 128 × 128 focal plane array detector. The spectral resolution was set to 8 cm–1 using a 25x objective with an optical resolution of 0.7 μm pixel size accumulating 80 scans per pixel. Measurements were done in reflection mode within the spectral region of 3500–950 cm–1. Background measurements (120 scans per pixel) were taken from a clean area (no cells) on the slide using the same acquisition parameters and subtracted from the respective spectra to compensate for atmospheric interference and instrument performance. Scanning was carried out using Agilent Resolutions Pro Software (Agilent Technologies, Santa Clara, CA, USA).
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9

Micro-Transmission FTIR Imaging Protocols

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Micro-transmission FTIR images were collected using an Agilent imaging system consisting of a Cary 670 FTIR spectrometer, coupled to a Cary 620 IR microscope with a 0.62 NA, 15 × Cassegrain objective, and a liquid nitrogen-cooled 128 × 128 focal plane array (FPA) detector with 5.5 × 5.5 μm2 pixel size. The system was used in “high magnification” mode, with magnifying optics before the FPA detector, providing an additional 5× magnification corresponding to 1.1 × 1.1 μm2 pixel size. For each mosaic image, 2 × 2 tiles were measured with 256 scans at 4 cm-1 spectral resolution in the 3900–1000 cm-1 spectral region. A background, measured in the absence of a sample (clean area of the calcium fluoride substrate), was also measured for each sample with 512 scans. Each mosaic image had an acquisition time of approximately 50 min.
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10

Characterization of Organic Compounds

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All solvents used were of reagent grade. Tryptone tryptophan medium, beef extract powder, peptone bacteriological, and soy peptone were purchased from Biolife. Agar and yeast extract were purchased from Fluka Analytical. Sodium chloride, D (+)-glucose, and di potassium hydrogen phosphate trihydrate were purchased from Merck. Dulbecco's modified Eagle's medium, (DMEM), fetal bovine serum, glutamine and trypsin were purchased from Gibco, Glasgow, UK. Phosphate buffer saline (PBS) was purchased from Sigma-Aldrich. Melting points were measured in open tubes with Stuart Scientific apparatus and are uncorrected. IR spectra in the region of 4000-370 cm -1 were obtained using a Cary 670 FTIR spectrometer, Agilent Technologies. A UV-1600 PC series spectrophotometer of VWR was used to obtain electronic absorption spectra. The 1 H NMR spectra were recorded using a Bruker AC 250, 400 MHFT-NMR instrument in DMSO-d 6 . ESI-MS spectra were recorded with an Agilent 1100/LC-MS system. 119 Sn Mössbauer spectra were recorded at various sample tempera-
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