: Robust and reproducible large-scale label-free deep quantitative profiling of the MOLM-14 surfaceome using three mass spectrometry platforms over multiple years

ABSTRACT: Surface proteins are one of the most important and common matrices for clinical chemistry and proteomic analyses. With the rapid developments in mass spectrometry (MS)-based proteomics methods, label-free quantitative proteomics has become an increasingly popular tool for profiling global protein abundances. Here, we evaluate the performance of three mass spectrometers, namely Orbitrap Elite (Hybrid Ion Trap-Orbitrap), Q Exactive HF (Hybrid Quadrupole-Orbitrap) and Orbitrap Fusion (Tribrid Quadrupole-Ion Trap-Orbitrap), in label-free semiquantitative analysis of cell surface proteins spanning a four-year period. Sucrose gradient ultracentrifugation was used for surfaceome enrichment, following gel separation for in-depth protein identification. With the established workflow, we identify 2335 cell surface proteins in MOLM-14, a human acute myeloid leukemia cell line, with a high degree of reproducibility across three MS platforms over multiple years.

INSTRUMENT(S): Orbitrap Fusion, Q Exactive HF, LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Richard Aplenc  

LAB HEAD: Richard Aplenc

PROVIDER: PXD022721 | Pride | 2021-12-30

REPOSITORIES: Pride