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Mascot 2.2 engine

Manufactured by Matrix Science
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Sourced in United Kingdom

The Mascot 2.2 engine is a high-performance laboratory equipment designed for a wide range of applications. It is a compact and powerful engine that can be used to drive various types of laboratory equipment and instruments. The Mascot 2.2 engine is known for its reliable performance and efficiency.

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Lab products found in correlation

Proteome discover 1, by Thermo Fisher Scientific (1 mentions) Proteome discoverer 1, by Thermo Fisher Scientific (1 mentions)

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Mascot (941 citations) Mascot 2.4 (358 citations) MASCOT engine (167 citations) Mascot search engine version 2.5 (19 citations) Mascot 2.0 search engine (7 citations) MASCOT engine v.2.2 (6 citations) Mascot 2.4 search engine (3 citations) Mascot 2.2 search engine (3 citations) Mascot 2.4.1 search engine (2 citations) Mascot 2.3 search engine (2 citations)

2 protocols using mascot 2.2 engine

1

Proteomic Analysis with Mascot and Proteome Discover

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The Mascot 2.2 engine (Matrix Science, London, UK) and Proteome Discover 1.4 (Thermo Scientific) were used to identify proteins and quantify phosphopeptides. More details were described in our previous study [23 (link)].
Wang X., Wang H., Li J., Li L., Wang Y, & Li A. (2023). Salt-induced phosphoproteomic changes in the subfornical organ in rats with chronic kidney disease. Renal Failure, 45(1), 2171886.
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2

Proteomic Analysis of Human Samples

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Analysis of MS/MS raw spectra was performed using MASCOT 2.2 engine (Matrix Science, UK) embedded into Proteome Discoverer 1.4 software (Thermo Scientific, USA)17 (link) against the UniprotKB human database (154,711 total entries, http://www.uniprot.org, Accessed 5 January 2017). The mass spectrometer was set at positive ion mode. Peptide mass tolerance was defined as ± 20 ppm, and the fragment mass tolerance was set as 0.1 Da. Proteins with at least one peptide above 95% confidence level and a threshold of false discovery rate (FDR) set to 0.01 were identified.18 (link) The ratio of relative abundance for proteins at weeks 14 and 0 was calculated, and proteins whose ratio were ≥1.2 or ≤0.8 folds were subjected to statistical analysis by significance A using Perseus, and proteins with P ≤ 0.05 were considered as DEPs.
Chen J., Li S., Ge Y., Kang J., Liao J.F., Du J.F., Tian J., Xie X, & Li F. (2021). iTRAQ and PRM-Based Proteomic Analysis Provides New Insights into Mechanisms of Response to Triple Therapy in Patients with Rheumatoid Arthritis. Journal of Inflammation Research, 14, 6993-7006.
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