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Direct detect infrared spectrometer

Manufactured by Merck Group
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The Direct Detect Infrared Spectrometer is a laboratory instrument that utilizes infrared spectroscopy to analyze the molecular composition of samples. It provides a rapid, accurate, and non-destructive method for identifying and quantifying various chemical compounds within a sample.

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Lab products found in correlation

Protease inhibitor cocktail, by Merck Group (6 mentions) Phosphatase inhibitor cocktail 2, by Merck Group (6 mentions) Milliplex analyst 5, by Merck Group (5 mentions) Odyssey clx scanner, by LI COR (5 mentions) Licor tbs blocking buffer, by LI COR (4 mentions) Nupage 4 12 bis tris gel, by Thermo Fisher Scientific (4 mentions) Anti flag, by Merck Group (3 mentions) Polyvinylidene difluoride membrane, by Merck Group (3 mentions) Mouse multiplex magnetic bead kits, by Thermo Fisher Scientific (2 mentions) High sensitivity mouse multiplex magnetic bead kit, by Merck Group (2 mentions) Anti ha, by Cell Signaling Technology (2 mentions) Iblot2 device, by Thermo Fisher Scientific (2 mentions) Chemidoc touch imaging system, by Bio-Rad (2 mentions) Anti β actin, by Abcam (2 mentions) Oasis cartridge, by Waters Corporation (2 mentions) Nd 1000 spectrophotometer, by Thermo Fisher Scientific (2 mentions) Halt protease and phosphatase inhibitor cocktail, by Thermo Fisher Scientific (2 mentions) Cylindrical quartz cuvette, by Hellma (2 mentions) Immun blot low fluorescent pvdf membrane, by Bio-Rad (2 mentions) Ne per nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (2 mentions)

Spelling variants of this product

Direct Detect Spectrometer (52 citations) Direct Detect (34 citations) Direct Detect® Infrared Spectrometer for Total Protein Quantitation (3 citations)

57 protocols using direct detect infrared spectrometer

1

Purification of AVR-Pik and HMA Proteins

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AVR-Pik effector proteins were produced with a cleavable Nt SUMO tag and a non-cleavable Ct His tag from pOPIN-E (58) in E. coli SHuffle (59) and purified as previously described (29) . HMA domains were produced with a cleavable Nt His-MBP tag from pOPIN-M in E. coli SHuffle. Pikp-HMA and Pikm-HMA were produced and purified as previously described (29) . For production of OsHIPP19-HMA, inoculated 1L cell cultures were grown in autoinduction media (60) at 30°C. 1 mM TCEP was included in the buffer for the final gel filtration of OsHIPP19-HMA. Protein concentration was determined using a Direct Detect ® Infrared Spectrometer (Millipore Sigma).
Maidment J.H.R., Franceschetti M., Maqbool A., Saitoh H., Jantasuriyarat C., Kamoun S., Terauchi R., & Banfield M.J. (2020). Multiple variants of the blast fungus effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19 with high affinity.
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2

Protein-Inhibitor Binding Detection

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To register new vibrations that could correspond to a formation of binding between potential inhibitors and protein, mixture of protein and each inhibitor stock was prepared with total volume of 40 µL. Stock solution of CA IX in a quantity of 20 µL, while the volume of inhibitor stock varied according to the molar ratios and water was added till the final volume. Prepared samples (2 µL) were spotted to assay free-membrane card, let to dry and inserted to Direct Detect Infra-red Spectrometer (Millipore Sigma, USA).
Žuvela P., Liu J.J., Yi M., Pomastowski P.P., Sagandykova G., Belka M., David J., Bączek T., Szafrański K., Żołnowska B., Sławiński J., Supuran C.T., Wong M.W, & Buszewski B. (2018). Target-based drug discovery through inversion of quantitative structure-drug-property relationships and molecular simulation: CA IX-sulphonamide complexes. Journal of Enzyme Inhibition and Medicinal Chemistry, 33(1), 1430-1443.
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3

Validating Antibody Specificity in Stroke Samples

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To authenticate the specificity of BACE1 and NRG1 type III antibodies, white matter regions (thalamus/internal capsule) were dissected from stroked mouse brains and sonicated in ice-cold 0.1 M phosphate buffered saline (PBS) containing 1% triton X-100 and 0.1% sodium deoxycholate, Protease Inhibitor Cocktail (1:100; Millipore Sigma), and Phosphatase Inhibitor Cocktail 2 (1:100; Millipore Sigma). Following centrifugation, the total protein concentration of each supernatant was measured using a Direct Detect Infrared Spectrometer (Millipore Sigma). Samples were then resolved by electrophoresis, transferred to a nitrocellulose membrane, and probed with the same BACE1 or NRG1 type III antibodies used for immunostaining throughout the manuscript: rabbit anti-BACE1 (1:1000, Cell Signaling) and rabbit anti-NRG1 type III (1:1000, Abcam). Following incubation with the appropriate secondary antibodies, proteins were visualized using a chemiluminescence detection system (GE Healthcare Life Sciences).
Nguyen T.V., Hayes M., Zbesko J.C., Frye J.B., Congrove N.R., Belichenko N.P., McKay B.S., Longo F.M, & Doyle K.P. (2018). Alzheimer’s associated amyloid and tau deposition co-localizes with a homeostatic myelin repair pathway in two mouse models of post-stroke mixed dementia. Acta Neuropathologica Communications, 6, 100.
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4

Protein Quantification in Mouse Tissues

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Snap-frozen brain and heart tissue samples (n = 5–11 mice/experimental group) were sonicated in ice-cold 0.1 M PBS containing 1% Triton X-100 and 0.1% sodium deoxycholate, Protease Inhibitor Cocktail (1:100; Millipore Sigma), and Phosphatase Inhibitor Cocktail 2 (1:100; Millipore Sigma). Following centrifugation, 13,000 × g at 4°C for 15 min, the total soluble protein concentration of each supernatant was measured using a Direct Detect Infrared Spectrometer (MilliporeSigma). Total MMP, OPN, and cytokines/chemokines concentrations were then measured using mouse multiplex magnetic bead kits (Milliplex Multiplex Assays, Millipore Sigma), according to the manufacturer’s protocols and recommendations. Each lysate sample, standard, and quality control were measured in duplicate. Plates were read using a MAGPIX instrument (Luminex), and results were analyzed using MILLIPLEX Analyst 5.1 software (Millipore Sigma).
Chung A.G., Frye J.B., Zbesko J.C., Constantopoulos E., Hayes M., Figueroa A.G., Becktel D.A., Antony Day W., Konhilas J.P., McKay B.S., Nguyen T.V, & Doyle K.P. (2018). Liquefaction of the Brain following Stroke Shares a Similar Molecular and Morphological Profile with Atherosclerosis and Mediates Secondary Neurodegeneration in an Osteopontin-Dependent Mechanism. eNeuro, 5(5), ENEURO.0076-18.2018.
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5

Quantification of Brain Proteins

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Snap-frozen brain tissue samples were sonicated in ice-cold 0.1 M PBS containing 1% triton-X and 0.1% sodium deoxycholate, Protease Inhibitor Cocktail (1:100; Millipore Sigma), and Phosphatase Inhibitor Cocktail 2 (1:100; Millipore Sigma). Following centrifugation, the total protein concentration of each supernatant was measured using a Direct Detect Infrared Spectrometer (Millipore Sigma). Total immunoglobulin G (IgG), matrix metalloproteinases (MMPs), albumin, and cytokines and chemokines were then quantified using mouse multiplex magnetic bead kits purchased from Thermo Fisher Scientific and Millipore Sigma, and used according to the manufacturer’s recommendations. Each lysate sample, standard, and quality control was measured in duplicate. Plates were read using a MAGPIX instrument (Luminex), and results were analyzed using MILLIPLEX Analyst 5.1 software (Millipore Sigma).
Zbesko J.C., Nguyen T.V., Yang T., Frye J.B., Hussain O., Hayes M., Chung A., Day W.A., Stepanovic K., Krumberger M., Mona J., Longo F.M, & Doyle K.P. (2018). Glial scars are permeable to the neurotoxic environment of chronic stroke infarcts. Neurobiology of disease, 112, 63-78.
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6

Quantification of Cytokines/Chemokines in Stroke

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At 3 weeks after surgery, infarcts from stroked mice and the equivalent region of the cortex from sham-operated mice were dissected and sonicated in ice-cold 0.1 M phosphate buffered saline containing 1% triton X-100 and 0.1% sodium deoxycholate, Protease Inhibitor Cocktail (1:100; Millipore Sigma), and Phosphatase Inhibitor Cocktail 2 (1:100; Millipore Sigma). After centrifugation, the total protein concentration of each supernatant was measured using a Direct Detect Infrared Spectrometer (Millipore Sigma). Cytokines/chemokines were then quantified by multiplex immunoassay using a high sensitivity mouse multiplex magnetic bead kit (Millipore Sigma) and performed according to the manufacturer’s recommendations (MILLIPLEX MAP Mouse Cytokine/Chemokine Magnetic Bead Panel-Immunology Multiplex Assay, MCYTOMAG-70K). Each lysate sample, standard, and quality control were measured in duplicate. Plates were read using a MAGPIX instrument (Luminex, Austin, TX), and results were analyzed using MILLIPLEX Analyst 5.1 software (Millipore Sigma). For those analytes that were below the lower limit of detection, the lower limit of detection values was used for data analysis. Concentrations of cytokines/chemokines were normalized to concentrations of total protein in the lysates.
Nguyen T.V., Crumpacker R.H., Calderon K.E., Garcia F.G., Zbesko J.C., Frye J.B., Gonzalez S., Becktel D.A., Yang T., Tavera-Garcia M.A., Morrison H.W., Schnellmann R.G., Longo F.M, & Doyle K.P. (2022). Post-Stroke Administration of the p75 Neurotrophin Receptor Modulator, LM11A-31, Attenuates Chronic Changes in Brain Metabolism, Increases Neurotransmitter Levels, and Improves Recovery. The Journal of Pharmacology and Experimental Therapeutics, 380(2), 126-141.
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7

Multiplex Cytokine Profiling in Stroke

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At 3 weeks following surgery, infarcts from stroked mice and the equivalent region of the cortex from sham operated mice were dissected and sonicated in ice cold 0.1 M phosphate buffered saline containing 1% triton X-100 and 0.1% sodium deoxycholate, Protease Inhibitor Cocktail (1:100; Millipore Sigma), and Phosphatase Inhibitor Cocktail 2 (1:100; Millipore Sigma). Following centrifugation, the total protein concentration of each supernatant was measured using a Direct Detect Infrared Spectrometer (Millipore Sigma). Cytokines/chemokines were then quantified by multiplex immunoassay using a high sensitivity mouse multiplex magnetic bead kit (Millipore Sigma) and performed according to the manufacturer's recommendations (MILLIPLEX MAP Mouse Cytokine/Chemokine Magnetic Bead Panel-Immunology Multiplex Assay, MCYTOMAG-70K). Each lysate sample, standard, and quality control were measured in duplicate. Plates were read using a MAGPIX instrument (Luminex, Austin, TX), and results were analyzed using MILLIPLEX Analyst 5.1 software (Millipore Sigma). For those analytes that were below the lower limit of detection, the lower limit of detection values was used for data analysis. Concentrations of cytokines/chemokines were normalized to concentrations of total protein in the lysates.
Nguyen T.V., Crumpacker R.H., Calderon K., Garcia F.G., Zbesko J.C., Frye J.B., Gonzalez S., Becktel D.A., Yang T., Tavera-Garcia M.A., Morrison H.W., Schnellmann R.G., Longo F.M., & Doyle K.P. (2021). Post-stroke administration of the p75 neurotrophin receptor modulator, LM11A-31, attenuates chronic changes in brain metabolism, increases neurotransmitter levels, and improves recovery.
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8

Quantification of Brain Proteins

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Snap-frozen brain tissue samples were sonicated in ice-cold 0.1 M PBS containing 1% triton-X and 0.1% sodium deoxycholate, Protease Inhibitor Cocktail (1:100; Millipore Sigma), and Phosphatase Inhibitor Cocktail 2 (1:100; Millipore Sigma). Following centrifugation, the total protein concentration of each supernatant was measured using a Direct Detect Infrared Spectrometer (Millipore Sigma). Total immunoglobulin G (IgG), matrix metalloproteinases (MMPs), albumin, and cytokines and chemokines were then quantified using mouse multiplex magnetic bead kits purchased from Thermo Fisher Scientific and Millipore Sigma, and used according to the manufacturer’s recommendations. Each lysate sample, standard, and quality control was measured in duplicate. Plates were read using a MAGPIX instrument (Luminex), and results were analyzed using MILLIPLEX Analyst 5.1 software (Millipore Sigma).
Zbesko J.C., Nguyen T.V., Yang T., Frye J.B., Hussain O., Hayes M., Chung A., Day W.A., Stepanovic K., Krumberger M., Mona J., Longo F.M, & Doyle K.P. (2018). Glial scars are permeable to the neurotoxic environment of chronic stroke infarcts. Neurobiology of disease, 112, 63-78.
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9

Production and Purification of Effector and HMA Proteins

Cited 1 time
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AVR-Pik effector proteins were produced with a cleavable Nt SUMO tag and a noncleavable Ct His tag from pOPIN-E (58 ) in E. coli SHuffle (59 (link)) and purified as previously described (29 ). HMA domains were produced with a cleavable Nt His-MBP tag from pOPIN-M in E. coli SHuffle. Pikp-HMA and Pikm-HMA were produced and purified as previously described (29 ). For production of OsHIPP19-HMA, inoculated 1 l cell cultures were grown in autoinduction media (60 (link)) at 30 °C. One millimolar TCEP was included in the buffer for the final gel filtration of OsHIPP19-HMA. Protein concentration was determined using a Direct Detect Infrared Spectrometer (Millipore Sigma).
Maidment J.H., Franceschetti M., Maqbool A., Saitoh H., Jantasuriyarat C., Kamoun S., Terauchi R, & Banfield M.J. (2021). Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defense. The Journal of Biological Chemistry, 296, 100371.
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10

NK Cell Activation and Signaling

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Freshly isolated NK cells were maintained overnight under standard conditions and were stimulated with human recombinant IL-15 (45 ng/mL, PeproTech, NJ, USA), DMOG (20 μM, Selleck Chemicals), rapamycin (25 nM, Merck Chemicals GmbH, Darmstadt, Germany), STAT3 inhibitor (S3I-201, 200 μM, Merck Chemicals GmbH), or DMSO (Sigma-Aldrich Chemie GmbH) as control, on the next day for the indicated time periods. Protein concentrations in cell lysates were determined on a Direct Detect® infrared spectrometer (Merck Millipore) according to the manufacturer's instructions.
Coulibaly A., Bettendorf A., Kostina E., Figueiredo A.S., Velásquez S.Y., Bock H.G., Thiel M., Lindner H.A, & Barbarossa M.V. (2019). Interleukin-15 Signaling in HIF-1α Regulation in Natural Killer Cells, Insights Through Mathematical Models. Frontiers in Immunology, 10, 2401.
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