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Raman station 400f

Manufactured by PerkinElmer
Sourced in United States, United Kingdom

The Raman Station 400F is a compact and versatile Raman spectrometer designed for a variety of laboratory applications. It features a high-performance optical system and a sensitive detector to provide accurate and reliable Raman spectroscopic analysis. The Raman Station 400F is capable of generating Raman spectra for a wide range of samples, allowing users to identify and characterize materials with precision.

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17 protocols using raman station 400f

1

Chemical Analysis of MRSA Strains

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In order to confirm the presence of particular chemical moieties in MRSAMupS as well as MRSAMupRL cells, FTIR and Raman spectroscopy analyses were carried out. After the cultivation of these strains for 18 h at 37 °C on Columbia agar with 5% sheep blood, the cells were washed three times by 5 mL of PBS, centrifuged at 5000 for 5 min, and dried for 24 h at 37 °C. The FTIR spectra of bacterial cells dry samples were obtained at room temperature by attenuated total reflection with a FTIR spectrometer (Perkin Elmer Spectrophotometer 100, Waltham, MA, USA). The samples (100 mg) were then scanned at a range between 650 cm−1 and 4000 cm−1 (64 scans and 1 cm−1 resolution). The obtained spectra were normalized, baseline corrected, and analyzed using SPECTRUM software (v10, Perkin Elmer Spectrophotometer, Waltham, MA, USA).
To obtain Raman spectra, the samples were analyzed using a Raman spectrometer (RamanStation 400F, Perkin Elmer, USA) with point and shot capability using an excitation laser source at 785 nm (to avoid fluorescence excitation), 100 micron spot size, 4 shots, and 8 s exposition time. The obtained spectra were normalized, baseline corrected, and analyzed using SPECTRUM software (v10, Perkin Elmer, Waltham, MA, USA).
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2

Characterization of Ferroelectric Materials

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All the SEM and EDS results are derived from the microscope (FEI, Quanta 450) integrated with the instrument (INCA Energy 200). The contact angles are measured by the goniometer (OCA25, Dataphysics). The crystallinity is characterized by the XRD (Rigaku Smartlab) and the Raman spectrometer (Perkinelmer Raman station 400F). The ferroelectricity is conducted on an Asylum Research MFP-3D Infinity AFM.
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3

FTIR and Raman Analysis of Klebsiella Pneumoniae

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In order to confirm the presence of particular chemical moieties in K. pneumoniaeCol-S and K. pneumoniaeCol-R, as well as in their LPS, FTIR and Raman spectroscopic analyses, were performed [18 (link)]. After 18 h cultivation of each strain at 37 °C on Columbia agar with 5% sheep blood, bacterial colonies were harvested, transferred to an Eppendorf tube, and washed three times using saline. Then, the samples were centrifuged at 5000× g for 5 min and dried for 24 h at 37 °C. The FTIR spectra of dried bacterial cell samples and freeze-dried LPS were obtained at room temperature by an attenuated total reflection FTIR spectrometer (Perkin Elmer Spectrophotometer 100, Waltham, MA, USA). The samples (100 mg) were then scanned at a range between 650 cm−1 and 4000 cm−1 (64 scans and 1 cm−1 resolution). The obtained spectra were normalised, baseline corrected, and analysed using SPECTRUM software (v10, Perkin Elmer Spectrophotometer, Waltham, MA, USA).
To obtain Raman spectra, the samples were analysed using the Raman spectrometer (RamanStation 400F, Perkin Elmer, Waltham, MA, USA) with point and shot capability and excitation laser source at 785 nm (to avoid fluorescence excitation), 100-micron spot size, and 4 scans (8 s exposition time). The obtained spectra were normalised, baseline corrected and analysed using SPECTRUM software (v10, Perkin Elmer, Waltham, MA, USA).
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4

Comprehensive Analysis of Bi(III) Solutions

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The surface morphology was analyzed with a scanning electron microscope (ESEM Tescan 500 PA) equipped with an energy‐dispersive X‐ray (EDX) analyzer (INCA x‐act Oxford Instruments) for determining the elemental composition. X‐ray diffraction (XRD) was performed with an X‐ray powder diffractometer (Bruker D8 advance, CuKα wavelength of 1.5406 Å). Raman spectra of the BiIII solutions were recorded with a Horiba Jobin Yvon confocal Raman microscope with a λ=633 nm focused laser beam. Due to the strong fluorescence of [SnCl3],61 these measurements were performed in a PerkinElmer Raman Station 400F with a focused λ=785 nm (NIR) laser. Quartz cuvettes with a path length of 2 mm were filled with electrolyte (1 mL) in the glove box, closed with a Teflon cap, and sealed with Parafilm. Five 30 s scans were recorded for each sample. 119Sn{1H} NMR spectra were recorded from a 10 mm solution of [NnBu4][SnCl3] in 12CE containing a D2O capillary as lock and TbCl3 as a relaxation agent. Data acquisition used a Bruker AVII400 spectrometer and chemical shifts are referenced to SnMe4 (δ=0 ppm).
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5

Raman and SERS Imaging of Phage-AuNP Hydrogel

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Raman Spectrum and NIR-SERS imaging of either targeted CGSPGWVRC-phage AuNP hydrogel or control insertless phage AuNP hydrogel were taken at a Raman Station 400F (Perkin-Elmer) with an excitation laser at 785 nm. The background was taken with the same volume of pure water and was subtracted from the results. CT images were acquired on a micro-CT Explore Locus RS-9 scanner (General Electric Medical Systems).
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6

Raman Spectroscopy of SERS Substrates

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Each substrate after static volatile collection was placed on the stage of a Raman spectroscopy instrument (RamanStation 400 F, Perkin-Elmer, Beaconsfield, Buckinghamshire, UK), which consists of a 256 × 1024 pixel CCD detector and a 175-mW near-infrared (785 nm) laser. All representative spectra that were averaged from seven different spots of the obtained SERS substrate were collected in quadruplicate with 2 s of exposure at a spectral resolution of 4 cm−1 in the Raman shift range of 200 to 2000 cm−1. All collected spectra were exported from built-in software (The Spectrum v. 6.3, Perkin-Elmer, Beaconsfield, Buckinghamshire, UK) and finally processed with baseline correction and normalization in MATLAB’s bioinformatics toolbox.
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7

Characterization of CD-Capped AuNPs

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Transmission Electron Microscopy (TEM) images were taken using a Philips CM200UT. The CD-capped AuNP monolayers deposited on quartz were investigated by scanning electron microscopy (SEM, JEOL JSM6700F). The average size of the CD-capped AuNPs was calculated using Fiji image processing software (ImageJ). The hydrodynamic diameters and the zeta-potentials of the AuNPs were measured by using a dynamic light scattering (DLS) and zeta-potential measurement system (Zetasizer NanoZS, Malvern Instruments). Optical extinction spectra of the CD-capped AuNP dispersion and CD-capped AuNP monolayer were obtained using a UV-vis spectrometer (JASCO V670). SERS was carried out using a Raman spectrometer (PerkinElmer Raman station 400F). The excitation wavelength was 785 nm, and the integration time was 300 s.
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8

SERS-based Quantification of RAD54 Protein

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Example 3

SERS spectra were acquired by Raman Spectro-microscope (Raman station 400F and microscope 300 from Perkin Elmer) using Spectrum software. The number of spectra per sample was 10 and spectral acquisition, number×time of exposure was 2×3 sec. Spectral pre-processing, including background subtraction, baseline correction and compression was done using the built-in Spectrum software.

The spectra were analyzed by multivariate PCA-LDA (principle component analysis and linear discriminant analysis) using the leave-one-out cross validation model. The levels of RAD54 protein were measured using the SERS-linked immunosensor assay and RAD54 levels expressed in response to H2O2 were correlated to EPA 3-tier guideline levels, IDLHs (for Immediately Dangerous to Life and Health concentrations) as determined by the Center for Disease Control and Prevention (CDC).

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9

Surface Characterization of Nanoparticles

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The surface morphology was analyzed using field-emission scanning electron microscopy (FE-SEM; Tescan LYRA 3) at a 20 kV accelerating voltage with a secondary electron detector. The NP distribution was generated from 50 NPs randomly measured from a FE-SEM micrograph. Energy dispersive X-ray spectroscopy (EDX, Brucker XFlash) coupled to the FE-SEM was used for the chemical analysis. Raman spectroscopy (Raman Station 400F Perkin-Elmer) was applied at RT using a 785 nm diode laser beam at a power of 15 mW. The water contact angle (WCA) was quantified using an automated tensiometer (Theta Attension; Biolin Scientific), placing a 5 µL droplet of deionized water at RT and 45% relative humidity.
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10

Raman Spectroscopic Analysis of SPI

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The 10 g of samples of SPI at different storage periods were solubilized 100 mL of deionized water at a concentration of 100 mg/mL for Raman spectroscopy analysis. The Raman spectroscopy analysis was determined according to the method of Zhu et al. [16 (link)], using PerkinElmer Raman Station 400 F dispersive Raman spectrometer equipped with a 785 nm diode laser under 80 mW of laser power. The laser was focused on the samples on glass slides. For each sample, the spectrum measurement with 60 s exposure time was repeated 10 times scan for each sample under 2 cm−1 resolution, and the spectral range was set to 400~2000 cm−1. Each sample was scanned three times, and the average spectrum was used for a representative spectrum for each sample.
Quantitative analysis on the secondary structure of SP under specific conditions was performed by Gaussian fitting using the Peakfit 4.12 software (Seasolve Software, Framingham, MA, USA). Raman spectra (400–2000 cm−1) were plotted as relative intensity (arbitrary units) against Raman shift (wavenumber (cm−1)).
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