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tunable pulsed quantum cascade laser  (DRS Daylight Solutions)


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    DRS Daylight Solutions tunable pulsed quantum cascade laser
    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A <t>tunable</t> <t>quantum</t> <t>cascade</t> <t>laser</t> (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.
    Tunable Pulsed Quantum Cascade Laser, supplied by DRS Daylight Solutions, used in various techniques. Bioz Stars score: 97/100, based on 566 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pulsed+quantum+cascade+laser+mircat+2400/MIRcat/pmc12823395-231-7-14
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    1) Product Images from "Label-free protein-structure-sensitive live-cell microscopy for patient-specific assessment of myeloma therapy"

    Article Title: Label-free protein-structure-sensitive live-cell microscopy for patient-specific assessment of myeloma therapy

    Journal: Nature Biomedical Engineering

    doi: 10.1038/s41551-025-01443-3

    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A tunable quantum cascade laser (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.
    Figure Legend Snippet: a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A tunable quantum cascade laser (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.

    Techniques Used: Modification, Comparison, Spectroscopy, Imaging, Micro-PAT

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    Article Title: Mapping enzyme activity in living systems by real-time mid-infrared photothermal imaging of nitrile chameleons.
    Article Snippet: The mid-infrared pump is provided by a pulsed quantum cascade laser (MIRcat 2400, Daylight Solutions) tunable from 900 cm−1 to 2,300 cm−1.

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    Article Snippet: This can be, for example, a pulsed quantum cascade laser from MIRcat 2400, Daylight Solutions, or the like.

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    Article Snippet: The mid-infrared pump is provided by a pulsed quantum cascade laser (MIRcat 2400, Daylight Solutions) with tunable range from 900 cm −1 to 2300 cm −1 .



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    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A <t>tunable</t> <t>quantum</t> <t>cascade</t> <t>laser</t> (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.
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    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A <t>tunable</t> <t>quantum</t> <t>cascade</t> <t>laser</t> (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.
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    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A <t>tunable</t> <t>quantum</t> <t>cascade</t> <t>laser</t> (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.
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    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A <t>tunable</t> <t>quantum</t> <t>cascade</t> <t>laser</t> (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.
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    Image Search Results


    a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A tunable quantum cascade laser (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.

    Journal: Nature Biomedical Engineering

    Article Title: Label-free protein-structure-sensitive live-cell microscopy for patient-specific assessment of myeloma therapy

    doi: 10.1038/s41551-025-01443-3

    Figure Lengend Snippet: a , Illustration of the amide I mid-IR spectrum of proteins (1,700–1,600 cm −1 ) showing the absorption bands of different secondary structures. Modified from ref. . b , Comparison of mid-IR absorption spectra of haemoglobin measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Haemoglobin is an α-helix protein with a characteristic band at 1,650 cm −1 (ref. ). c , Comparison of mid-IR absorption spectra of concanavalin A measured by MiROM (blue line) and standard ATR-FTIR spectroscopy (red line). Concanavalin A is a homotetramer protein with a β-sheet structure and characteristic absorption bands at 1,622, 1,634 and 1,691 cm −1 (ref. ). d , Comparison of mid-IR absorption spectra of haemoglobin (red line) and concanavalin A (blue line) measured by MiROM. e , Comparison of mid-IR absorption spectra of albumin in the native state (primarily α-helix, blue line) and denatured state (primarily β-sheet, red line). The vertical dashed lines indicate the α-helix absorption peak at 1,654 cm −1 and the intermolecular β-sheet absorption peak at 1,612 cm −1 . f , Schematic diagram of the MiROM imaging system. A tunable quantum cascade laser (QCL) provides excitation for optoacoustic imaging, while a focused ultrasound (US) transducer is used for signal readout. g – i , MiROM micrographs of live HeLa cells imaged at 1,645 cm −1 in cell media composed of different H O/D O proportions. j , Contrast-to-noise ratio (CNR) profile of HeLa cells in g – i . The contrast profile in 100% D O is 3.4 times higher than that in pure H O, while the contrast profile in 70% D O is 2.2 times higher than that in pure H O. The observed apparent shift in the contrast profile is caused by cell movements between measurements. k , Normalized spectra in the amide I region of live HeLa cells in 70% D O medium acquired at the points highlighted by the arrows in h . The vertical dashed lines indicate the turn, α-helix and β-sheet secondary structure absorption peaks (see Supplementary Table ). l , Each coloured line represents the second derivative of the spectrum in the same colour in k . The scheme above the plot details the values corresponding to the different secondary structures according to the literature . n = 3 independent experiments. OA, optoacoustic; NOA, normalized optoacoustic.

    Article Snippet: OA signals are generated using a broadly tunable pulsed quantum cascade laser (QCL, MIRcat, Daylight Solutions).

    Techniques: Modification, Comparison, Spectroscopy, Imaging, Micro-PAT