Ground steel target

Manufactured by Bruker

Sourced in Germany

The ground steel target is a laboratory equipment item designed for use in various analytical techniques. It serves as a stable and uniform surface for sample placement and analysis. The product is made of high-quality steel that has been precisely ground to ensure a flat and consistent surface. This ground steel target is a versatile tool that can be utilized in a range of laboratory applications.

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Lab products found in correlation

Protein calibration standards 1, by Bruker (3 mentions) Maldi tof tof mass spectrometer, by Bruker (3 mentions) Flexanalysis, by Bruker (2 mentions) Flexcontrol, by Bruker (2 mentions) Maldi tof biotyper, by Bruker (1 mentions) C18 ziptip, by Merck Group (1 mentions) Chemidoc xrs system, by Bio-Rad (1 mentions) Maldi tof ms, by Bruker (1 mentions) Ultraflextreme mass spectrometer, by Bruker (1 mentions) Mass frontier, by Thermo Fisher Scientific (1 mentions) 2 5 dihydroxybenzoic acid matrix, by Bruker (1 mentions) Protein calibration standards 1 and 2, by Bruker (1 mentions)

Close spelling variants of this product

MTP 384 ground steel target plate MSP 96 BC ground steel target 384-well ground steel target MSP96 target ground steel BC Ground Steel massive 384 target plate MSP 96 target ground steel Ground Steel MALDI target Ground steel MALDI target plate MTP 384 ground steel target plate TF Ground steel target plate

10 protocols using ground steel target

MALDI-TOF Identification of E. coli

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The suspect E. coli colonies from McConkey agar were identified by a matrix-assisted laser desorption/ionization (MALDI-TOF) biotyper (Bruker Daltonics, Leipzig, Germany). Bacterial extracts for mass spectrometry measurements were prepared as recommended by the manufacturer of the MS instrument. For MALDI-TOF analysis, one colony was spotted onto a ground steel target (Bruker Daltonik GmbH, Leipzig, Germany) and air dried for 15 min.
Each sample spot was overlaid with 2 μl of matrix solution (saturated solution of α-cyano-4-hydroxy-cinnamic acid in 50% acetonitrile with 2.5% trifluoroacetic acid), and again air dried for 15 min. To identify the relevant microorganisms, the raw spectra obtained for each isolate were imported into a BioTyper software, version 2.0 (Bruker Daltonik GmbH, Leipzig, Germany), and analysed without any user intervention^{10 (link)}.

Gregova G, & Kmet V. (2020). Antibiotic resistance and virulence of Escherichia coli strains isolated from animal rendering plant. Scientific Reports, 10, 17108.

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MALDI-TOF analysis of AgUox variants

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Purified AgUox-WT and AgUox-frTet variants (0.4 mg/mL) were digested with trypsin. The trypsin-digested mixture was desalted using ZipTip C18 (Millipore, Billerica, MA, USA). The desalted trypsin-digested protein sample was mixed with 2,5-dihydroxybenzoic acid (DHB) solution (20 mg/mL of DHB in 3:7, (v/v) acetonitrile: 0.1% trifluoroacetic acid in water) in a 1:1 ratio. Then, 0.5 μL of this mixture was loaded onto a ground steel target (Bruker Corporation, Billerica, MA, USA) and molecular weight analysis was performed by MALDI-TOF MS (Bruker Corporation, Billerica, MA, USA).
To identify the IEDDA reactivity of the AgUox-frTet variants, purified AgUox-WT and AgUox-frTet variants were desalted with phosphate-buffered saline (PBS, pH 7.4) and then mixed with TCO-Cy3 at a molar ratio of 1:2 for 2 h at room temperature. Afterwards, the mixture, with or without the addition of TCO-Cy3, was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The gel underwent fluorescence analysis (excitation: 302 nm, filter 510/610 nm) in a ChemiDoc XRS+ System (Bio-Rad Laboratories, Hercules, CA, USA), followed by visualization after Coomassie brilliant blue (CBB) staining.

Yang B, & Kwon I. (2021). Thermostable and Long-Circulating Albumin-Conjugated Arthrobacter globiformis Urate Oxidase. Pharmaceutics, 13(8), 1298.

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LDI-TOF-MS Analysis of ZnO Nanocrystals

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The LDI-TOF-MS analysis was performed using ultrafleXtreme mass spectrometer (Bruker Daltonics, Hamburg, Germany) and ZnO NCs suspended in water were spotted on the ground steel target (Bruker Daltonik, Bremen, Germany) according to the previously described protocol [10 (link)] with the required modification (without the α-Cyano-4-hydroxycinnamic acid (HCCA) matrix). Protein Calibration Standards I (Bruker Daltoniks, Bremen, Germany), Peptide Calibration Standard and two signals characteristic for the matrix [M-H]⁺ and [2M-H]⁺ were used for the external calibration, according to the standardized Bruker sample preparation procedure. Molecular fingerprint (MF) spectra of ZnO NCs were recorded in reflectron positive mode, within a m/z range of 100–3500, and we applied an acceleration voltage of 25 kV. Fragment spectra were recorded using the LIFT default method (Bruker Daltonics, Hamburg, Germany) at 100% of laser power, global attenuator 50% with calibration on the immonium ions [29 (link),30 (link)]. The voltage on the LIFT electrodes was 19.0 and 2.7 kV, respectively. MS spectra were registered in FlexControl (Bruker Daltonics, Hamburg, Germany), while the FlexAnalysis (Bruker Daltonics, Hamburg, Germany) was used for data analysis.

Pomastowski P., Król-Górniak A., Railean-Plugaru V, & Buszewski B. (2020). Zinc Oxide Nanocomposites—Extracellular Synthesis, Physicochemical Characterization and Antibacterial Potential. Materials, 13(19), 4347.

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MALDI-TOF/TOF-MS Analysis of Inhibitors

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0.5 µL of the mixture prepared for SDS-PAGE measurements for each inhibitor was spotted to ground steel target (Bruker Daltonics, Germany) with saturated solution of α-Cyano-4-hydroxycinnamic acid as a matrix using dried droplet technique. Mass spectra were obtained using MALDI-TOF/TOF-MS (Bruker Daltonics, Bremen, Germany) equipped with a modified neodymium-doped yttrium aluminum garnet (Nd: YAG) laser operating at the wavelength of 355 nm and frequency of 2 kHz. Results were obtained in linear positive mode with the mass range of 15,000–60,000 (m/z) with a laser power of 60% and global attenuator offset of 50%. Recorded spectra were smoothed using weighted adjacent-averaging with periodic boundary condition.

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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GAG Disaccharide Derivatization and MALDI-TOF Analysis

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The derivatization solution consisted of 2-AA (Figure 1(a1)) that was dissolved in methanol/acetic acid (9:1, v/v) at a concentration of 0.025 mmol/mL. Then, 1 μL of GAG disaccharide solution was applied onto a ground steel target (Bruker Daltonics, Bremen, Germany). After the spot dried, 1 μL of derivatization solution was applied onto the sample and the plate was heated for 2 h at 65 °C. After the plate cooled down, 1 μL of matrix solution (10 mg/mL super-DHB in 50% ACN) was pipetted onto the sample and the target was allowed to dry at room temperature.

Krüger L., Biskup K., Karampelas V., Ludwig A., Kasper A.S., Poller W.C, & Blanchard V. (2022). Straightforward Analysis of Sulfated Glycosaminoglycans by MALDI-TOF Mass Spectrometry from Biological Samples. Biology, 11(4), 506.

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MALDI-TOF MS/MS Metabolite Identification

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Compounds were tentatively identified by accurate mass match of obtained high resolution FT-ICR m/z values to the Metlin database [41 ]. Identifications were confirmed using MALDI-TOF MS/MS on matrix coated barley tissue sections or on methanolic extracts. For extracts, 2 mg to 40 mg of freeze-dried, milled tissue were extracted with 1 ml water by ribolysing (3 x 45 s, 15 min pause, 6.5 m/s) using 500 mg ribobeads (0.5 mm diameter, Roth) for tissue disruption. Samples were centrifuged 15 min at 14,000 rpm. 1 μl to 2 μl of the supernatant were spotted on a ground steel target (Bruker Daltonics) with 1 μl 2,5-dihydroxybenzoic acid matrix (30 mg/ml in 50% methanol, 0.2% TFA). Dextrin 20 (Serva) with a concentration of 1 mg/ml was used as a reference sample for oligosaccharide analysis. The MALDI-TOF was calibrated on peptide standards. MS/MS was performed on selected precursor ions with individual laser settings using collision induced dissociation (CID) with argon as collision gas at a pressure of 2 x 10⁶ mbar and a collision energy of 8 keV. The software functions Mass frontier (Thermo scientific) and IsotopePattern (Bruker Daltonics) served for structure and formula elucidation of metabolites.

Gorzolka K., Kölling J., Nattkemper T.W, & Niehaus K. (2016). Spatio-Temporal Metabolite Profiling of the Barley Germination Process by MALDI MS Imaging. PLoS ONE, 11(3), e0150208.

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Rapid Microbial Species Identification via MALDI-TOF MS

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Species identi cation of pyomelanin pigment producer Streptomyces strain was carried out with MALDI TOF/TOF MS (Bruker Daltonics, Auto ex Speed). For this purpose, mass signals from most abundant and conserved ribosomal protein fractions that are speci c at genus, species or sub-group levels was detected. MALDI-TOF MS log (score) values range between 2.3-3.000 was interpreted as highly probable species-level identi cation and values range between 2.000-2.299 was interpreted as secure genus identi cation and probable species identi cation. For the extraction of ribosomal protein, formic acid method which was applied by Bizzini et al. ( 2010) was used and samples were prepared for MS analysis.
The samples taken from a single bacterial colony using a sterile wood applicator were transferred to the steel target plate (Ground Steel Target, Bruker Daltonics). Transferred microorganisms were overlaid with 1.0 μL of a saturated HCCA matrix (a solution of α-cyano-4-hydroxycinnamic acid in 50% acetonitrile -2.5% tri uoroacetic acid -CAS Number 28166-41-8). To allow co-crystallization, the sample was kept for drying at room temperature (Bizzini et al. 2010 ). Mass spectra were calibrated with the recommended BTS (Bacterial Test Standard) for MS (See Supplementary Figure 1).

Bayram S. (2021). Extracellular Pyomelanin Pigment Production, Purification and Characterization with Streptomyces griseus MPPS2.

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MALDI-TOF Mass Spectrometry Biosilver Analysis

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All chemicals for the MALDI MS analyses were supplied at the highest commercially available purity by Fluka Feinchemikalien (Neu-Ulm, Germany; a subsidiary of Sigma-Aldrich). Ground steel targets (Bruker Daltonik, Bremen, Germany) were used for sample deposition. The α-cyano-4-hydroxycinnamic acid (HCCA) was employed as matrix for MALDI analysis of biosilver spotted by dried droplet method (Pomastowski et al. 2015 ). Protein Calibration Standards I (Bruker Daltoniks, Bremen) and HCCA were used for external calibration. All the MS spectra were obtained using the MALDI–TOF/TOF mass spectrometer (Bruker Daltonik, Bremen, Germany) equipped with a modified Nd:YAG laser operating at the wavelength of 355 nm and frequency of 2 kHz. The system was controlled using the Bruker Daltonik software (flexControl and flexAnalysis). Molecular fingerprint (MF) spectra of silver biocolloids were recorded in reflectron positive mode, within an m/z range of 100–3500, and applying an acceleration voltage of 25 kV.

Viorica R.P., Pawel P., Kinga M., Michal Z., Katarzyna R, & Boguslaw B. (2017). Lactococcus lactis as a safe and inexpensive source of bioactive silver composites. Applied Microbiology and Biotechnology, 101(19), 7141-7153.

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MALDI-TOF MS Analysis of Intact Proteins

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The MALDI-TOF MS analyses were performed using chemicals at the highest commercially available purity supplied by Fluka Feinchemikalien (a subsidiary of Sigma-Aldrich, NeuUlm, Germany). Ground steel targets (Bruker Daltonik, Bremen, Germany) were used for sample deposition and the sinapinic acid was employed as matrix for MALDI analysis of intact proteins (dried droplet method) [28 (link)]. Protein Calibration Standards I and II (Bruker Daltoniks, Bremen, Germany) were used for external calibration. All the MS spectra were obtained using the MALDI-TOF/TOF mass spectrometer (Bruker Daltonik, Bremen, Germany) equipped with a modified neodymium-doped yttrium aluminum garnet (Nd:YAG) laser operating at the wavelength of 355 nm and frequency of 2 kHz. The system was controlled using the Bruker Daltonik software (flexControl and flexAnalysis). MS spectra of intact proteins were obtained in the linear positive mode in an m/z range of 15,000–30,000, applying an acceleration voltage of 25 kV. All mass spectra were acquired and processed using dedicated software flexControl and flexAnalysis, respectively (both from Bruker Daltonik).

Pryshchepa O., Sagandykova G.N., Pomastowski P., Railean-Plugaru V., Król A., Rogowska A., Rodzik A., Sprynskyy M, & Buszewski B. (2019). A New Approach for Spontaneous Silver Ions Immobilization onto Casein. International Journal of Molecular Sciences, 20(16), 3864.

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MALDI-TOF/TOF Mass Spectrometry Protocol

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The matrix [α cyano-4-hydroxycinnamic acid (HCCA)] and silver samples were deposited on ground steel targets (Bruker Daltonics, Bremen, Germany) by the spotted dried droplet method [13 (link)]. All reagents were purchased from Fluka Feinchemikalien (Neu-Ulm, Germany). The experiments were performed with a MALDI-TOF/TOF mass spectrometer (Bruker Daltonics, Bremen, Germany) in tandem with a modified neodymium-doped yttrium aluminium garnet laser operated at 355 nm and 2 kHz.
Protein Calibration Standards I (Bruker Daltonics, Bremen, Germany) and HCCA were used for calibration:

Railean-Plugaru V., Pomastowski P., Kowalkowski T., Sprynskyy M, & Buszewski B. (2018). Physicochemical study of natural fractionated biocolloid by asymmetric flow field-flow fractionation in tandem with various complementary techniques using biologically synthesized silver nanocomposites. Analytical and Bioanalytical Chemistry, 410(11), 2837-2847.

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