Peptide mixture

Manufactured by Bruker

The Peptide Mixture is a laboratory equipment product that contains a pre-formulated combination of various peptides. It is designed to serve as a standard reference material for the identification, characterization, and quantification of peptides in analytical applications.

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Lab products found in correlation

Ultraflextreme maldi tof tof mass spectrometer, by Bruker (2 mentions) Maldi plate, by Bruker (1 mentions)

Close spelling variants of this product

Peptide standard mixture Peptide calibration standard mixture Peptide calibration mixture

3 protocols using peptide mixture

MALDI-TOF MS Lipid Profiling Protocol

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MALDI-TOF MS was performed using an UltrafleXtreme MALDI-TOF/TOF mass spectrometer (Bruker Daltonik; Bremen, Germany). The TOF was calibrated using a peptide mixture (Bruker Daltonik) before acquisition of the sample spectra. The dried lipid extracts were reconstituted in 200 μl of CHCl₃/MeOH (2:1, v/v). Equal volume (1–2 μl) of lipid extract and MALDI matrix solution (0.5 M 2,5-dihydroxybenzoic acid, DHB, in methanol containing 0.1% trifluoroacetic acid) was mixed in a 0.6-ml microcentrifuge tube. Then, 1 μl of the mixture was spotted onto a MALDI plate (Bruker Daltonik). The mass spectra were acquired over the m/z range of 0–1,000 in both positive and negative ion Reflectron TOF modes. The laser power was adjusted to a point just above the ionization threshold of the sample, and the laser rate was set at 10 Hz with 1,000 laser shots per acquisition. Ten acquisitions were averaged for each individual sample.
Tandem mass spectrometry (MS/MS) analysis was performed on molecular species of interest (some major abundant lipid classes) using LIFT-TOF/TOF mode. The product ions characteristic head-group of the lipid was used to identify the lipid class. Fragment ions were generated by LIFT (laser ionization fragmentation technology) approach as described previously15 (link).

Tipthara P, & Thongboonkerd V. (2016). Differential human urinary lipid profiles using various lipid-extraction protocols: MALDI-TOF and LIFT-TOF/TOF analyses. Scientific Reports, 6, 33756.

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Lipidomic Analysis of Extracellular Vesicles

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Each of the TLC bands visualized from microvesicular or exosomal sample was scrapped from the silica plate, resuspended in 2:1(v/v) chloroform/methanol and analyzed using UltrafleXtreme MALDI-TOF/TOF mass spectrometer (Bruker Daltonik; Bremen, Germany) as previously described^{41 (link)}. Briefly, the TOF was calibrated using a peptide mixture (Bruker Daltonik) before acquisition of the sample spectra. Equal volume (1–2 µl) of lipid extract and MALDI matrix solution (0.5 M 2,5-dihydroxybenzoic acid in methanol containing 0.1% trifluoroacetic acid) was mixed in a 0.6-ml microcentrifuge tube. Then, 1 µl of the mixture was spotted onto a MALDI plate. The mass spectra were acquired over the m/z range of 0–2,000 in positive ion Reflectron TOF mode. The laser power was adjusted to a point just above the ionization threshold of the sample, and the laser rate was set at 10 Hz with 1,000 laser shots per acquisition. A total of 10 acquisitions were averaged for each sample.

Singhto N., Vinaiphat A, & Thongboonkerd V. (2019). Discrimination of urinary exosomes from microvesicles by lipidomics using thin layer liquid chromatography (TLC) coupled with MALDI-TOF mass spectrometry. Scientific Reports, 9, 13834.

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Clickable Glycopeptide Enrichment

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The SGP standard was first dissolved in 0.1 M sodium acetate to make a stock solution at 1 mg/mL. Then, 100 μl stock solution was mixed with NaIO₄ to the final concentration of 1 mM. HA-tag was dissolved in DMSO at 1 M and added into the solution at 1:50 ratio. The resulting mixture was desalted using Sep-Pak C18 column to remove excess reagents, before spiking into a peptide mixture (Bruker, Daltonics). Then click chemistry was performed on either Dde-Azide agarose or PEG-azide resin. Briefly, the peptide mixture was incubated with solid phase material with 0.1 mM CuSO₄, 0.5 mM THPTA and 5 mM sodium ascorbate for 12 h at 4 °C with end-to-end rotation. The sample was then centrifuged, and the resin was washed with PBS buffer and water twice with vortexing to remove nonspecific binding peptides. 5% hydrazine was added to the resin for elution and incubated for 4 h before the supernatant was collected and dried prior to analysis. Samples were taken in each step for MALDI or ESI-MS/MS analysis. For the isotopic labeling study, a similar workflow was conducted on SGP standard or (Glc)₈ as described above, isotopic reagent hydrazine sulfate (¹⁵N₂H₄ H₂SO₄) was treated with stoichiometric NaOH to free isotopic hydrazine (¹⁵N₂H₄) first before adding to release SGP or exchange hydrazone.

Li M., Huang J., Ma M., Shi X, & Li L. (2022). Selective Enrichment of Sialylglycopeptides Enabled by Click Chemistry and Dynamic Covalent Exchange. Analytical chemistry, 94(18), 6681-6688.

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