Maldi 7090

Manufactured by Shimadzu

Sourced in Japan

The MALDI-7090 is a matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometer. It is a laboratory instrument used for the analysis and identification of biomolecules, such as proteins, peptides, and oligonucleotides, through accurate mass measurement.

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Lab products found in correlation

Ultraflextreme maldi tof tof, by Bruker (2 mentions) Prominence hplc, by Shimadzu (1 mentions) Readyprep protein extraction kit, by Bio-Rad (1 mentions) Synergy h4, by Agilent Technologies (1 mentions) Uv 3600, by Shimadzu (1 mentions) Lumina fluorescence spectrometer, by Thermo Fisher Scientific (1 mentions) N n diisopropylethylamine dipea, by Merck Group (1 mentions) A300 10 12, by Bruker (1 mentions)

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MALDI-7090 TOF-TOF mass spectrometer (2 citations) MALDI-TOF 7090 (2 citations)

12 protocols using maldi 7090

Peptide Synthesis and Characterization

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The peptides designed in this study were synthesized by GL Biochem (Shanghai, China). The precise molecular mass was confirmed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) (MALDI-7090, Shimadzu Kratos, Manchester, UK). The purity of designed peptides was determined by reverse-phase high performance liquid chromatography (RP-HPLC) (LC3000, Beijing, China) on a Gemini-NX C18 column (250 × 4.60 mm, with 5 μm internal particles) and the detection wavelength was 220 nm. All these peptides had a purity higher than 95%.
Primary peptide sequence analyses were performed using the bioinformatics programs ProtParam (ExPASy Proteomics Server: http://web.expasy.org/protparam/). Charge and grand average of hydropathicity (GRAVY) were calculated online using HeliQuest (http://heliquest.ipmc.cnrs.fr/cgi-bin/ComputParamsV2.py) and ExPASy (https://web.expasy.org/protparam/).

Yang Y., Wu D., Wang C., Shan A., Bi C., Li Y, & Gan W. (2020). Hybridization with Insect Cecropin A (1–8) Improve the Stability and Selectivity of Naturally Occurring Peptides. International Journal of Molecular Sciences, 21(4), 1470.

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Ethylenediamine Functionalization of BSA

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First, 500 mg BSA (dissolved in 5.0 mL distilled water), and 150 mg EDCI·HCl were added to 40 mL 1.4 M ethylenediamine solution (pH = 4.75) and stirred at room temperature for 2 h. Then, 400 μL 4 M acetate buffer (pH = 4.75) was added to terminate the reaction. The product was purified by bag filter (molecular cut off: 7 kDa) to remove free ethylenediamine and EDCI. Water was removed by freeze-drying. The product was analyzed by MALDI-TOF–MS (Shimadzu MALDI-7090).

Li Y., Shi S., Ming Y., Wang L., Li C., Luo M., Li Z., Li B, & Chen J. (2018). Specific cancer stem cell-therapy by albumin nanoparticles functionalized with CD44-mediated targeting. Journal of Nanobiotechnology, 16, 99.

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MALDI-MS Protein Analysis Protocol

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MALDI-MS was performed using a MALDI-TOF/TOF ultrafleXtreme (Bruker-Daltonics) equipped with a 1 kHz laser or a MALDI-7090 (Shimadzu) equipped with a 2 kHz laser, both operated in linear positive-ion mode. A total of 5,000 shots were summed using a 100 µm laser diameter and a user optimised laser intensity. Samples were prepared using the matrix 3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoic acid (sinapinic acid) and dissolved in a mixture of TA30 (30% acetonitrile and 70% water with trifluoroacetic acid (0.1% v/v)). 1 µL of each protein was initially combined with 10 µL of matrix before spotting 2 µL of the sample onto a ground steel plate or AnchorChip target. External calibration was achieved with bovine serum albumin (BSA) using the average mass of the [M+H] + m/z ~66.5 kDa and [M+2H] 2+ m/z ~33.3 kDa (Supplementary Table 1). Acquired spectra were exported to the opensource software mMass for processing (Supplementary Table 1 and2).

Teo S.L.Y., Rennick J.J., Yuen D., Al-Wassiti H., Johnston A.P.R., & Pouton C.W. (2020). Unravelling cytosolic delivery of endosomal escape peptides with a quantitative endosomal escape assay (SLEEQ).

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Quantitative Proteomic Profiling of Liver

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The liver samples were subjected to proteomic analysis. Liver samples were prepared using Ready Prep Protein Extraction kit (Bio-Rad) at first. Extracted protein concentration was determined by BioSpec-nano (Shimadzu Biotech, Kyoto). Approximately 4 mg of protein/group was used for quantitative proteomic profiling. NBS tagging was performed according to the manufacturer’s protocol (13CNBS stable isotope labeling kit; Shimadzu). Briefly, each solution (each containing 400 µg of protein) was labeled with isotopically ¹²C6NBS or ¹³C6NBS reagent. NBS-tagged proteins were then mixed, reduced, alkylated, and digested by trypsin. NBS-tagged peptides were enriched and separated by 2D-nano HPLC (Prominence HPLC, Shimadzu) as described previously (49 (link)). Eluates were automatically deposited onto MALDI target plates by the LC spotting system (AccuSpot; Shimadzu Biotech, Kyoto). These spotted samples were automatically analyzed by MALDI-TOF/TOF MS (MALDI-7090, Shimadzu Kratos, Manchester, UK).

Feng Q., Yao J., Zhou G., Xia W., Lyu J., Li X., Zhao T., Zhang G., Zhao N, & Yang J. (2018). Quantitative Proteomic Analysis Reveals That Arctigenin Alleviates Concanavalin A-Induced Hepatitis Through Suppressing Immune System and Regulating Autophagy. Frontiers in Immunology, 9, 1881.

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Protein Characterization by MALDI-MS

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MALDI-MS was performed using a MALDI-TOF/TOF ultrafleXtreme (Bruker-Daltonics) equipped with a 1 kHz laser or a MALDI-7090 (Shimadzu) equipped with a 2 kHz laser, both operated in linear positive-ion mode. A total of 5000 shots were summed using a 100-µm laser diameter and a user optimised laser intensity. Samples were prepared using the matrix 3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoic acid (sinapinic acid) and dissolved in a mixture of TA30 (30% acetonitrile and 70% water with trifluoroacetic acid (0.1% v/v)). Then, 1 µL of each protein was initially combined with 10 µL of matrix before spotting 2 µL of the sample onto a ground steel plate or AnchorChip target. External calibration was achieved with bovine serum albumin (BSA) using the average mass of the [M + H]⁺ m/z ~66.5 kDa and [M + 2H]²⁺ m/z ~33.3 kDa (Supplementary Table 2). Acquired spectra were exported to the open-source software mMass for processing (Supplementary Tables 2 and 3).

Teo S.L., Rennick J.J., Yuen D., Al-Wassiti H., Johnston A.P, & Pouton C.W. (2021). Unravelling cytosolic delivery of cell penetrating peptides with a quantitative endosomal escape assay. Nature Communications, 12, 3721.

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Analysis of FSHR Nitration by MALDI-TOF

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KGN cells were incubated with PN (100 nM, 12 hrs) and MG132 (30 μM, 4 hrs) followed by treatment with FSH (1 nM, 4 hrs). The cell lysates were subject to SDS-PAGE. FSHR bands were excised manually from CBB stained gels, destained with 100 mM Ammonium bicarbonate/50% Acetonitrile and dehydrated in Acetonitrile by vacuum drying. The dehydrated gel slices were subject to trypsin digestion. Tryptic digested peptides were extracted 50% Acetonitrile/0.1% trifluoroacetic acid (TFA). The extracted peptides were lyophilized and reconstituted in 0.1% TFA and desalted using MonoTip C18 Columns (Shimadzu GL). The desalted peptides were subject to MALDI-TOF MS analysis as previously described [51 (link)]. This raw data acquired by MALDI-7090 (Shimadzu Kratos) was then searched against SwissProt Database with possible modifications of single and double nitration on tyrosine (+45 Da for single nitration and +90 Da for double nitration) using MALDI Solutions following the instructions of the manufacturer [52 (link)].

Zhou G., Hu R.K., Xia G.C., Yan S.H., Ren Q.L., Zhao J., Wang F.H., Huang C.C., Yao Q., Tan Y, & Zhao N.W. (2019). Tyrosine nitrations impaired intracellular trafficking of FSHR to the cell surface and FSH-induced Akt-FoxO3a signaling in human granulosa cells. Aging (Albany NY), 11(10), 3094-3116.

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Synthesis and Characterization of RAP-DNA Conjugate

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5 OD PS‐DNA was dried under rotary evaporation. Then 2.2 mg RAP‐Bz‐Br dissolved in 0.1 mL DMSO was added and vibrated under 50 ℃ for 1 h. Then, deionized water was added into the mixture and washed by EA to remove free RAP‐Bz‐Br. The final RAP‐DNA conjugate was obtained after dried over. 15% denaturing PAGE electrophoresis was used to characterize the successful synthesis of RAP‐DNA. The molecule weight of RAP‐DNA was determined by matrix‐assisted laser desorption ionization time‐of‐flight mass spectrometry (MALDI‐TOF, Shimadzu MALDI 7090, Japan). To determine the critical micelle concentration (CMC) of RAP‐DNA, 1 µL Nile Red solution (100 × 10⁻⁶ m) dissolved in THF was added into 100 µL RAP‐DNA solution at a concentration range from 0.003 to 9 × 10⁻⁶ m in terms of DNA. After incubated for 2 h, the fluorescence intensity of Nile Red was determined on a microplate reader (Synergy H4, Biotek, USA) with the excitation/emission wavelengths of 543/620 nm. The CMC value was obtained at the concentration point that induce the rush of fluorescence intensity.

Guo Y., Qin J., Zhao Q., Yang J., Wei X., Huang Y., Xie M., Zhang C, & Li Y. (2022). Plaque‐Targeted Rapamycin Spherical Nucleic Acids for Synergistic Atherosclerosis Treatment. Advanced Science, 9(16), 2105875.

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Gel-based Protein Identification and Characterization

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The band of interest was excised from the gel and rinsed three times with Milli-Q water. The band was then cut into approximately 1-mm² pieces and dried. The gel slices were reduced with 30 μL of 10-mM DTT at 56 °C for 60 min and cooled down to RT. Sixty microliters of 100-mM iodoacetamide was added and the protein was alkylated for 45 min at RT in the dark. Subsequently, the gel slices were completely dried and added to a trypsin solution to incubate at 37 °C overnight. After the reaction was cooled down to RT, the supernatant was removed and saved. The gel was subsequently extracted with 100 μL 0.1% and 5% TFA in 50% ACN by gently mixing and incubated at RT for 15 min, respectively. Each wash was combined with the saved supernatant, and the resulting solution was lyophilizated for further MALDI-TOF/TOF (MALDI-7090, Shimadzu Kratos) analysis. The peptide mass fingerprints and peptide ion MS/MS spectra were acquired on MALDI-7090. The total MS/MS data was searched against SwissProt database using the following parameters: trypsin digestion allowing up to 2 missed cleavages, fixed modifications of cysteine (carbamidomethylation), variable modifications of methionine (oxidation) and lysine (β-hydroxybutyrylation), precursor peptide tolerance of 0.05 Da, and MS/MS tolerance of 0.2 Da. Search results with e values less than 0.01 were judged as positive identifications.

Guo J., Wang Y., Tang L., Tang T., Li Z., Li M., Wang L., Zeng A., Ma Y., Huang S., Jiang X, & Guo W. (2023). The regulation of Tfh cell differentiation by β-hydroxybutyrylation modification of transcription factor Bcl6. Chromosoma.

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Trx1 and TrxR Protein Interaction Assay

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First, 5 mM LH was incubated with 35 µg Human Trx1 protein (Sino Biological Inc., Beijing, China), and 3.3 mM LH was incubated with 4.8 µg Human TrxR protein (Cayman Chemical, Ann Arbor, MI, USA) for 2 h at 37 °C. All the protein samples were reduced by Shimadzu Biotech Proteome Kit, trypsin digested using MonoSpin Trypsin, and desalted by a MonoSpin C18 column, then detected by MALDI 7090 (SHIMADZU, Kyoto, Japan).

Zhang W., Zhu Y., Yu H., Liu X., Jiao B, & Lu X. (2021). Libertellenone H, a Natural Pimarane Diterpenoid, Inhibits Thioredoxin System and Induces ROS-Mediated Apoptosis in Human Pancreatic Cancer Cells. Molecules, 26(2), 315.

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Molecular Weight Determination of Laminarin and Fucoidan

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The molecular weight of both the laminarin and fucoidan were determined by the mass by charge ratio (m/z) analysed between 1000 and 10,000 m/z by MALDI-TOF analysis using MALDI-7090™ (SHIMADZU)^{43 (link)}.

Sanniyasi E., Gopal R.K., Damodharan R., Arumugam A., Sampath Kumar M., Senthilkumar N, & Anbalagan M. (2023). In vitro anticancer potential of laminarin and fucoidan from Brown seaweeds. Scientific Reports, 13, 14452.

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