Anchorchip maldi target plate

Manufactured by Bruker

Sourced in United States, Germany

The AnchorChip MALDI target plate is a specialized sample preparation device used in matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. It provides a uniform and efficient sample deposition platform for analyte analysis.

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Lab products found in correlation

Ultraflextreme mass spectrometer, by Bruker (1 mentions) Flexcontrol 3.4 software build 119, by Bruker (1 mentions) Maldi tof tof mass spectrometer, by Bruker (1 mentions) Biotools, by Bruker (1 mentions) Peptide calibration standard, by Bruker (1 mentions) 1 hydroxybenzotriazole hydrate hobt, by Merck Group (1 mentions) Sodium dodecyl sulphate (sds), by Merck Group (1 mentions) Peptide n glycosidase f, by Roche (1 mentions) Hplc supragradient acetonitrile acn, by Biosolve (1 mentions) 1 ethyl 3 3 dimethylaminopropyl carbodiimide hydrochloride edc, by Fluorochem (1 mentions) Purelab ultra, by Elga LabWater (1 mentions) Sodium hydroxide (naoh), by Merck Group (1 mentions) Flexanalysis, by Bruker (1 mentions) Flexcontrol, by Bruker (1 mentions)

5 protocols using anchorchip maldi target plate

Protein Identification by MALDI-TOF/TOF MS

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Those gel blocks stained with coomassie were
manually excised, transferred into a 1.5 ml Eppendorf
tube, destained using 2009L Milli-Q for 6 hours, and
finally digested with sequencing-grade modified 0.01
μg/μL trypsin (2-3 μL) at 37°C overnight. 1 μL of the
digested samples was eluted with an equal volume
of matrix solution α-Cyano-4-Hydroxycinnamic
Acid (HCCA, Sigma. USA) containing in 0.1%
trifluoroacetic acid (TFA) and 50% acetonitrile (ACN),
were dotted onto an AnchorChip™ MALDI target
plate (Bruker Daltonics, Billerica, MA, USA). Peptide
sequencing and protein identification were performed
by MALDI-TOF/TOF MS method on an AutoFlex III
mass spectrometer (BrukerDalton, Bremen, Germany)
working in reflection mode as previously described
(21 (link)). Polypeptide calibrator was used as an internal
reference.

Chen X., Liu Y., Zhu X, & Lv Q. (2021). Comparative Proteome Analysis Indicates The Divergence between The Head and Tail Regeneration in Planarian. Cell Journal (Yakhteh), 23(6), 640-649.

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MALDI-TOF-MS Glycan Structure Elucidation

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Released, derivatized, and purified glycans (5 µL sample) were spotted on an anchor chip MALDI target plate (Bruker Daltonics) and co-crystallized with 0.5 µL of 5 mg/mL superDHB in 50% can, supplemented with 1 mM NaOH. Spectra were recorded in positive-ion reflector mode, after calibration with a Bruker peptide calibration kit, using a Bruker UltrafleXtremeTM mass spectrometer, controlled by FlexControl 3.4 software Build 119 (Bruker Daltonics). Mass spectra were obtained over an m/z range of 1000 to 5000 for a total of 10 000 shots (1000 Hz laser frequency, 200 shots per raster spot during complete random walk). Tandem mass spectrometry (MALDI-TOF-MS/MS) was performed for structural elucidation via fragmentation in gas-off TOF/TOF mode.

Holst S., Wilding J.L., Koprowska K., Rombouts Y, & Wuhrer M. (2019). N-Glycomic and Transcriptomic Changes Associated with CDX1 mRNA Expression in Colorectal Cancer Cell Lines. Cells, 8(3), 273.

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Proteomic Identification of Carbonylated Proteins

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The protein and carbonylated protein that were corresponded the protein spot on 2D gels, were excised into 1-mm³ pieces from 2D gels and de-stained with 25 mM NH₄CO₃ in 50% acetonitrile. The gels were dehydrated by adding acetonitrile and then, digested with 25 μl of 0.1 mM trypsin in 25 mM NH₄CO₃ for 15 min51 (link). The excess trypsin solution was removed, and gel pieces were incubated at 37 °C overnight in 20 μl of 25 mM NH₄CO₃. A mixture of 1 μl peptide solution and 1 μl matrix solution with 1 mg ml⁻¹, a-cyano-4-hydroxycinnamic acid in 70% acetonitrile, and 0.1% trifluoroacetic acid was loaded onto the AnchorChip MALDI target plate (Bruker Daltonics, Manning Park Billerica, MA, USA) and analyzed by a matrix assisted laser desorption-ionization time of flight (MALDI-TOF)/TOF mass spectrometer (Bruker Daltonics), according to the manufacturer’s instructions. MS data were uploaded to the Mascot server using Biotools (Bruker Daltonics) and searched against the National Center for Biotechnology Information (NCBI) protein database (25,010,123 sequences; 8,625,376,125 residues; search parameters, rice; proteolytic enzyme, trypsin; maximum missed cleavages, 1; fix modifications, carbamidomethyl; variable modifications, oxidation; peptide mass tolerance, 100 ppm; fragment mass tolerance, 0.5 Da). Spots with a Mowse score higher than 65 were considered as proteins.

Yin G., Xin X., Fu S., An M., Wu S., Chen X., Zhang J., He J., Whelan J, & Lu X. (2017). Proteomic and Carbonylation Profile Analysis at the Critical Node of Seed Ageing in Oryza sativa. Scientific Reports, 7, 40611.

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Optimized Peptide Purification Protocol

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Sodium dodecyl sulphate (SDS), ethanol and trifluoroacetic acid were purchased from Merck (Darmstadt, Germany). Nonidet P-40 substitute (NP-40), super-DHB (9:1 mixture of 2,5-dihydroxybenzoic acid and 2-hydroxy-5-methoxybenzoic acid)43 , sodium hydroxide (NaOH) and 1-hydroxybenzotriazole hydrate (HOBt) were acquired from Sigma-Aldrich (Steinheim, Germany). 1-Ethyl-3-(3-(dimethylamino)propyl)carbodiimide hydrochloride (EDC) was acquired from Fluorochem (Hadfield United Kingdom). Peptide-N-glycosidase F (PNGase F) was supplied by Roche Diagnostics (Mannheim, Germany). Cotton thread was bought from Pipoos (Utrecht, The Netherlands). HPLC SupraGradient acetonitrile (ACN) was acquired from Biosolve (Valkenswaard, The Netherlands). Peptide calibration standard and an AnchorChip MALDI target plate were purchased from Bruker Daltonics (Bremen, Germany). Pooled plasma from 20 healthy human donors was purchased from Affinity Biologicals (Ancaster, Canada) and used as control sample. Lastly, water was purified with a Purelab Ultra from Elga LabWater (Ede, The Netherlands).

Jansen B.C., Bondt A., Reiding K.R., Lonardi E., de Jong C.J., Falck D., Kammeijer G.S., Dolhain R.J., Rombouts Y, & Wuhrer M. (2016). Pregnancy-associated serum N-glycome changes studied by high-throughput MALDI-TOF-MS. Scientific Reports, 6, 23296.

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MALDI-TOF/TOF Analysis of Lipid Extracts

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The extracted lipids were dissolved in 0.5 mL of methanol. The 10-mg (DHB and HCCA) matrix was dissolved in 1 mL of the mixed solution (30:70, acetonitrile: 0 .1 % TFA in water). Two microliters of the extracted lipid samples was mixed with 2 µL of either matrix, and this 1 µL of mixture sample/matrix was applied to spot on an AnchorChip MALDI target plate (anchor diameter 800 µm; Bruker Daltonik GmbH, Bremen, Germany). The mass spectra were calibrated using the cesium triiodide cluster. Each sample was analyzed 3 times. A MALDI-TOF/TOF MS instrument equipped with a modified neodymium-doped yttrium aluminum garnet (Nd: YAG) laser (1-kHz Smartbeam-II, Bruker Daltonik) operating at the wavelength of 355 nm was used for all measurements. All spectra were acquired in reflector positive mode using an acceleration voltage of 25 kV within a m/z range of 100 to 1,600 at 80% of laser power and global attenuator of 50%. All mass spectra were acquired and processed using dedicated software, flexControl and flexAnalysis, respectively (both from Bruker Daltonik).
All of the lipid species were identified by using the LIPID MAPS online database (http: / / www .lipidmaps .org/ ; Fahy et al., 2007) (link).

Walczak-Skierska J., Złoch M., Pauter K., Pomastowski P, & Buszewski B. (2020). Lipidomic analysis of lactic acid bacteria strains by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Journal of dairy science, 103(12).

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