Sequencing grade trypsin

Manufactured by G Biosciences

Sequencing Grade Trypsin is a highly purified, proteolytic enzyme used for the digestion of proteins. It is suitable for use in various applications, including protein sequencing, mass spectrometry, and protein sample preparation.

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Lab products found in correlation

Q tof api us quad tof mass spectrometer, by Waters Corporation (4 mentions) Nanoacquity uplc, by Waters Corporation (4 mentions) Atlantis c18 column, by Waters Corporation (2 mentions) Cem discover microwave digestor, by G Biosciences (1 mentions)

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Trypsin (9 citations)

4 protocols using sequencing grade trypsin

Mass Spectrometry Characterization of FadR_she

Cited 1 time

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The identity of the recombinant FadR_she protein we produced was confirmed using A Waters Q-Tof API-US Quad-ToF mass spectrometer connected to a Waters nano Acquity UPLC) (Feng & Cronan, 2011a (link)). In brief, the protein band of interest was cut from 15% SDS-PAGE gel, de-stained and digested with Sequencing Grade Trypsin (G-Biosciences St. Louis, MO, 12.5 ng/μL in 25 mmol/L ammonium bicarbonate); Second, the resulting peptides were loaded on a Waters Atlantis C-18 column (0.03 mm particle, 0.075 mm × 150 mm), following the further cleaning treatment. The data dependent acquisition combined with ms/ms analysis was routinely performed (Feng & Cronan, 2011a (link)).

Zhang H., Zheng B., Gao R, & Feng Y. (2015). Binding of Shewanella FadR to the fabA fatty acid biosynthetic gene: implications for contraction of the fad regulon. Protein & Cell, 6(9), 667-679.

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Identifying Recombinant Protein by Mass Spectrometry

Cited 2 times

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The identity of the recombinant BgaC protein was directly confirmed using A Waters Q-Tof API-US Quad-ToF mass spectrometer linked to a Waters nano Acquity UPLC as we performed earlier42 (link). The de-stained gel slice of interest was digested with 25 μl of Sequencing Grade Trypsin (G-Biosciences, St. Louis, MO, 12.5 ng μl⁻¹ in 25 mM ammonium bicarbonate) and the resultant peptides were extracted with 50% acetonitrile containing 5% formic acids. The mass spectrometer was applied for data acquisition and Waters Protein Lynx Global Server 2.2.5, Mascot (Matrix Sciences) combined with BLAST against NCBI nr database were subjected for data analysis43 (link).

Hu D., Zhang F., Zhang H., Hao L., Gong X., Geng M., Cao M., Zheng F., Zhu J., Pan X., Tang J., Feng Y, & Wang C. (2014). The β-galactosidase (BgaC) of the zoonotic pathogen Streptococcus suis is a surface protein without the involvement of bacterial virulence. Scientific Reports, 4, 4140.

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Recombinant AgaR1/AgaR2 Protein Identification

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To verify the identity of the recombinant AgaR1 (and/or AgaR2), the resultant peptides by digestion with Sequencing Grade Trypsin (G‐Biosciences, St. Louis, MO, 12.5 ng μL⁻¹ in 25 mmol/L ammonium bicarbonate) were subjected for analyses of A Waters Q‐Tof API‐US Quad‐ToF mass spectrometer linked to a Waters nano Acquity UPLC (Feng et al. 2013b). The mass data acquired were assayed through Waters Protein Lynx Global Server 2.2.5, Mascot (Matrix Science, Boston, MA, USA) combined with BLAST against NCBI nr database (Feng et al. 2014a).

Zhang H., Ravcheev D.A., Hu D., Zhang F., Gong X., Hao L., Cao M., Rodionov D.A., Wang C, & Feng Y. (2015). Two novel regulators of N‐acetyl‐galactosamine utilization pathway and distinct roles in bacterial infections. MicrobiologyOpen, 4(6), 983-1000.

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Identification of Recombinant PdhR Protein

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The identity of the recombinant PdhR protein was verified using a Waters Q-Tof API-US Quad-ToF mass spectrometer linked to a Waters Nano Acquity UPLC [14 (link)]. The destained SDS-PAGE gel slice was digested with 25 μl of Sequencing Grade Trypsin (G-Biosciences, St. Louis, MO, 12.5 ng /μl in 25 mM ammonium bicarbonate) using a CEM Discover Microwave Digestor (Mathews, NC) for 15 min at 55°C and 50 W. The resultant peptides were extracte d with 50% acetonitrile containing 5% formic acids, dried using a Savant SpeedVac and suspended in 20 μl of 5% acetonitrile containing 0.1% formic acid. The sample (~10 μl) was loaded on a Waters Atlantis C-18 column (0.03 mm particle, 0.075 mm by 150 mm) and eluted at a flow rate of 250 nl per min using a linear gradient of water/acetonitrile containing 0.1% formic acid 0–60% B in 60 min. Following data acquisition by the mass spectrometer, MS/MS analyses were conducted on the most abundant four peaks present at any given retention time. The Waters Protein Lynx Global Server 2.2.5, Mascot (Matrix Sciences) and the BLAST NCBI nr database was used for data processing [17 (link), 14 (link)].

Feng Y, & Cronan J.E. (2014). PdhR, the Pyruvate Dehydrogenase Repressor, Does not Regulate Lipoic Acid Synthesis. Research in microbiology, 165(6), 429-438.

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