Mtp 384 ground steel

Manufactured by Bruker

Sourced in Germany

The MTP 384 ground steel is a laboratory equipment product designed for precise sample preparation. It features a 384-well microplate format made of ground steel, providing a durable and scratch-resistant surface for various applications.

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Lab products found in correlation

Ultraflex 3 tof tof, by Bruker (2 mentions) Ultraflextreme mass spectrometer, by Bruker (2 mentions) Maldi plate, by Bruker (2 mentions) Autoflex 2 mass spectrometer, by Bruker (1 mentions) Ultraflex 3 maldi tof tof instrument, by Bruker (1 mentions) Zeba spin desalting column, by Thermo Fisher Scientific (1 mentions) Flexanalysis software, by Bruker (1 mentions) Prism 6, by GraphPad (1 mentions) α cyano 4 hydroxycinnamic acid, by Merck Group (1 mentions) Flexanalysis version 3, by Bruker (1 mentions) Clinprotool, by Bruker (1 mentions) Autoflex 3, by Bruker (1 mentions)

9 protocols using mtp 384 ground steel

MALDI-TOF MS Protocol for DNA Analysis

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The
matrix for MALDI-TOF MS was 1:1 mixture
of 3-hydroxypicolinic acid (3HPA) in 1:1 acetonitrile/H₂O saturated solution and 0.5 M ammonium citrate aqueous solution.
1 μL of DNA sample was mixed with 1 μL of matrix solution.
A spot of 1 μL of the sample–matrix mixture was placed
on a MALDI target plate (MTP 384 ground steel, Bruker) and allowed
to air dry at room temperature. The spectrum was measured using a
matrix-assisted laser desorption/ionization-time-of-flight mass spectrometer
(MALDI-TOF MS) on Bruker autoflex II mass spectrometer (negative mode)
with dT₈ ([M – H]⁻: 2370.603)
and dT₁₇ ([M – H]⁻: 5108.376)
as an external calibration standard.

Ishizuka T., Yamashita A., Asada Y, & Xu Y. (2017). Studying DNA G-Quadruplex Aptamer by 19F NMR. ACS Omega, 2(12), 8843-8848.

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MALDI-TOF/TOF Protein Identification Protocol

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The peptide mixture obtained was mixed in 1:1 ratio with 5 mg/ml HCAA in 1:2 ratio of 0.1% TFA and 100% ACN. Two microliters of sample was spotted onto the MALDI plate [(MTP 384 ground steel (Bruker Daltonics, Germany)]. The samples were analyzed on the MALDI-TOF/TOF ULTRAFLEX III instrument (Bruker Daltonics, Germany). FLEX ANALYSIS SOFTWARE (Version 3.3) was used to analyze the molecular weight of 500 laser shots with reflectron ion mode ranging between 500 and 5000 m/z for obtaining the MS-MS data. The masses obtained in the MS-MS were submitted for Mascot search in the “Viridiplantae” database to identify the protein (Koenig et al., 2008 (link)).

Nagamalla S.S., Alaparthi M.D., Mellacheruvu S., Gundeti R., Earrawandla J.P, & Sagurthi S.R. (2021). Morpho-Physiological and Proteomic Response of Bt-Cotton and Non-Bt Cotton to Drought Stress. Frontiers in Plant Science, 12, 663576.

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MALDI-TOF MS Protein Sample Preparation

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Protein samples were loaded into Zeba™ Spin Desalting Columns (Thermo Scientific Inc., USA) pre-equilibrated with water. The columns were centrifuged at 1500 rpm for 2 min and the desalted fraction was precipitated overnight with 2 volumes of cold acetone at −20 °C After centrifugation at 12,000 rpm for 15 min, the protein pellet was resuspended in 0.1 %TFA/50 %ACN to a final concentration of 10 μg/μL. The protein was mixed with MALDI matrix solution (10 mg sinapinic acid in 1 mL of 50 % acetonitrile containing 0.1 % trifluoroacetic acid), directly spotted onto the MALDI target (MTP 384 ground steel, Bruker Daltonik, GmbH), and allowed to dry at room temperature. MALDI-TOF MS spectra were collected using Ultraflex III TOF/TOF (Bruker Daltonik, GmbH) in linear positive mode with a mass range of 5000–100,000 Da. Five hundred shots were accumulated with a 200-Hz laser for each sample. MS spectra were analyzed by FlexAnalysis software (Bruker Daltonik, GmbH). Bovine insulin, equine cytochrome C and equine apomyoglobin were used as external protein calibrations.

Pechsrichuang P., Songsiriritthigul C., Haltrich D., Roytrakul S., Namvijtr P., Bonaparte N, & Yamabhai M. (2016). OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system. SpringerPlus, 5(1), 1200.

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MALDI-TOF MS Analysis of Sphingolipids

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Prior to MALDI TOF MS analysis, samples were spotted on an MTP 384 ground steel Bruker MALDI plate using the two-layer/overlay method: 0.4 μL of sample was deposited and allowed to dry, followed by deposition of 0.4 μL of matrix solution. Matrix solutions included 10 mg/mL of DHB and 10 mg/mL of THAP, with and without 10 mM LiCl_(aq). All matrix solutions were made in n-propanol/MeOH (1:1, v/v). MALDI TOF MS analysis was done using an ultrafleXtreme mass spectrometer (Bruker Daltonics, Bremen, Germany) in positive reflectron mode. Laser properties included a medium smartbeam at a frequency of 1 kHz for 6000 shots per sample. The laser power used was 62–64% for THAP and 50%–52% for DHB. Random walk, partial sample mode was enabled. The m/z range was set to 440–1600. Sphingomyelin and ceramide abundance were calculated using a one-point calibration curve based on the addition of the internal standard mixture (EquiSPLASH lipidomix, SM(d36:2-d9) and Cer(d33:1-d7)), respectively. The lithium adduct ([M + Li]⁺) was used for the calculation of abundance for both the analyte and internal standard. Data was analyzed via Bruker’s flexAnalysis Version 3.4 (Build 50). Univariate analysis was done using Prism 6 (GraphPad, La Jolla, CA).

Tran A., Wan L., Xu Z., Haro J.M., Li B, & Jones J.W. (2020). Lithium Hydroxide Hydrolysis Combined with MALDI TOF Mass Spectrometry for Rapid Sphingolipid Detection. Journal of the American Society for Mass Spectrometry, 32(1), 289-300.

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Quantification of HIV-1 Protease Activity

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Twenty μl of standard working solution of p17-p24 [dissolved in H₂O for Renin, Cathepsin D and HIV-1 protease or in acetate buffer (50 mM, pH 4.5) for BACE1] were added and incubated at 37 °C for 30 min. The determination of p17-p24 cleavage sites was carried out by MALDI-TOF. Briefly, 1 μl of sample was mixed with 1 μl of HCCA matrix [a saturated solution of α-cyano-4-hydroxycinnamic acid (Sigma) in 50/50/0.1% of water/acetonitrile/trifluoroacetic acid] and spotted on metal target plate (MTP 384 Ground Steel, Bruker). Mass spectra were acquired with 200 laser shots for sample at a constant laser energy in reflector mode and elaborate using Flex Analysis software.

Caccuri F., Iaria M.L., Campilongo F., Varney K., Rossi A., Mitola S., Schiarea S., Bugatti A., Mazzuca P., Giagulli C., Fiorentini S., Lu W., Salmona M, & Caruso A. (2016). Cellular aspartyl proteases promote the unconventional secretion of biologically active HIV-1 matrix protein p17. Scientific Reports, 6, 38027.

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MALDI-TOF MS Sample Preparation

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Prior to MALDI TOF MS analysis, samples were spotted on a MTP 384 ground steel Bruker MALDI plate using a dried-droplet spotting technique as described above. The same matrices used in the AP-MALDI experiments were used for the MALDI-TOF experiments. MALDI TOF MS analysis was done using an ultra-fleXtreme mass spectrometer (Bruker Daltonics, Bremen, Germany) in positive reflectron mode. Laser properties included medium smartbeam at a frequency of 1 kHz for 5000 shots per sample. Random walk, partial sample mode was enabled. The m/z range was set to 450–1600. Data was analyzed via Bruker’s flexAnalysis Version 3.4.

Tran A., Monreal I.A., Moskovets E., Aguilar H.C, & Jones J.W. (2021). Rapid Detection of Viral Envelope Lipids Using Lithium Adducts and AP-MALDI High-Resolution Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 32(9), 2322-2333.

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Protein Quantification and Peptide Analysis

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The protein concentration in serum was determined by the Lowry method (16 (link)). The absorbance at 750 nm (OD750) was measured, and the protein concentration was calculated using the standard curve, plotted between OD750 on Y-axis and BSA concentration (g/ml) on X-axis. The peptides from serum were acidified with 0.1% trifluoroacetic acid to the final concentration of 0.1 mg/ml. The peptides were mixed with MALDI matrix solution (10 mg sinapinic acid in 1 ml of 50% acetonitrile containing 0.1% trifluoroacetic acid), directly spotted onto MALDI target (MTP 384 ground steel, Bruker Daltonik, GmbH), and allowed to dry at room temperature. Maldi-TOF MS spectra were collected using Ultraflex III TOF/TOF (Bruker Daltonik, GmbH) in a positive linear mode with a mass range of 2,000–15,000 Da. Five hundred shots were accumulated with a 50 Hz laser for each sample. MS spectra were analyzed by using flexAnalysis and ClinproTool software (Bruker Daltonik, GmbH), including fingerprint spectra, pseudo-gel view, and principal component analysis (PCA). ACTH fragment 18–39 (human), Insulin oxidized B chain (bovine), Insulin (bovine), Cytochrome C (equine), and Apomyoglobin (equine) were used as external protein calibrations.

Sukumolanan P., Phanakrop N., Thaisakun S., Roytrakul S, & Petchdee S. (2021). Analysis of the Serum Peptidomics Profile for Cats With Sarcomeric Gene Mutation and Hypertrophic Cardiomyopathy. Frontiers in Veterinary Science, 8, 771408.

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Peptide Profiling via MALDI-TOF-MS

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The peptide profiles were analyzed by means of matrixassisted laser desorption/ionization time-of-flight mass spectrometry (Maldi-TOF-MS) using an Autoflex III mass spectrometer (Bruker Daltonics, Bremen, Germany) equipped with a 355 nmNd: YAG laser. The sample was mixed with matrix solution comprising 10 mg/mL of α-cyano-4hydroxycinnamic acid in 50% acetonitrile with 0.1% trifluoroacetic acid. Subsequently, 0.5 μL of this mixture was spotted onto a MALDI target plate (MTP 384 ground steel, Bruker Daltonics, Bremen, Germany) and dried at room temperature. The mass spectra were acquired in positive reflection mode using an acceleration voltage of 19 kV and a laser frequency of 100 Hz. The ion detection range was m/z 0.7 to 3 KDa. External calibration was performed using a standard mixture of peptides. The data were acquired using Flex Control software, and the spectra were processed using Flex Analysis One software (Version 3.0, Bruker Daltonics).

de Lima M.D.S.F., da Silva R.A., da Silva M.F., da Silva P.A.B., Costa R.M.P.B., Teixeira J.A.C., Porto A.L.F, & Cavalcanti M.T.H. (2018). Brazilian Kefir-Fermented Sheep's Milk, a Source of Antimicrobial and Antioxidant Peptides. Probiotics and antimicrobial proteins, 10(3).

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MALDI-MS Analysis of Philibertain G II

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The molecular mass and homogeneity of philibertain g II was determined by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). The sample was spotted on an MTP 384 GroundSteel and mixed with freshly prepared matrix solution (sinapic acid) and processed in a UltrafleXtrem MALDI-TOF mass spectrometer (Bruker Daltonics, Germany), using bovine carbonic anhydrase as standard.

Sequeiros C., Torres M.J., Nievas M.L., Caffini N.O., Natalucci C.L., López L.M, & Trejo S.A. (2016). The Proteolytic Activity of Philibertia gilliesii Latex. Purification of Philibertain g II. Applied biochemistry and biotechnology, 179(2).

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