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. 2021 Jul 29;2(5):zqab036. doi: 10.1093/function/zqab036

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© The Author(s) 2021. Published by Oxford University Press on behalf of American Physiological Society.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Identification of human AC8 (ADCY8; Swissprot ID: P40145; ADCY8_HUMAN Adenylate cyclase type 8) by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis in U87 cells but not HEK293 cells. (A) Summary of proteomic data sets generated by trypsin digestion and LC-MS/MS analysis of HEK293, HEK293 cells in which immuno-precipitation with anti-AC8 antibody had been carried out, U87 cells and U87 samples which had been obtained by immuno-precipitation. Shown are the number of protein groups quantified, total number of peptides identified, total number of unique peptides identified, number of AC8 peptides identified and number of unique AC8 peptides identified. All results were generated in MaxQuant (Andromeda search algorithm) and are displayed at a FDR of 1% (FDR 0.01), which was obtained through a target-decoy database search approach. The AC8-IP heading in the table denotes immune-precipitated AC8. (B) Quantified protein raw intensity as generated in MaxQuant software are compared for the different conditions. (C) The number of peptides specific to ADCY8 (AC8) using trypsin digestion are shown. (D) Data base searching (MASCOT algorithm) following isolation from U87 cell lysate by immunoprecipitation identified human ADCY8 with a protein score of 348 (FDR: 1%). Sequence coverage overview showing tryptic peptides detected in red font. Highlighted regions show cytoplasmic domains and transmembrane helices, respectively. The overall sequence coverage achieved is 17%; sequence coverage within the cytoplasmic domains is 24%.