Proteomics

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Immunoaffinity-free chromatographic purification of ovarian cancer biomarker CA125 (MUC16) from blood serum


ABSTRACT: The present work developed a non-affinity-based chromatographic method to enrich MUC16 from serum. The enriched MUC16 sample was further processed using a Midi Top 14 abundant protein depletion column. Peptides identified using bottom-up proteomics yielded 1–8% coverage of MUC16. Additionally, MUC16 was detected in samples containing less than the clinical cut-off level of CA125 (35 U/mL), suggesting that this strategy of enrichment and bottom-up proteomics can enable analysis of CA125 from serum of individuals with early-stage ovarian cancer and those whose tumors express CA125 (MUC16) at low levels.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

DISEASE(S): Malignant Neoplasm Of Ovary

SUBMITTER: Rebecca Whelan  

LAB HEAD: Rebecca Whelan

PROVIDER: PXD053289 | Pride | 2024-10-17

REPOSITORIES: Pride

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Publications

Immunoaffinity-free chromatographic purification of ovarian cancer biomarker CA125 (MUC16) from blood serum enables mass spectrometry characterization.

Schuster-Little Naviya N   Sokolovsky Andrew D AD   Gentry Ashten A   Saraf Anita A   Etzel Mark R MR   Patankar Manish S MS   Whelan Rebecca J RJ  

Analytical methods : advancing methods and applications 20240926 37


The enrichment of trace proteins from human fluid samples is of great importance in diverse clinical and industrial applications. In clinical diagnostics, such enrichment may enable detection of trace proteins that serve as biomarkers of disease. Affinity-based approaches, such as immunoaffinity pulldown, are widely used to enrich trace proteins, but this strategy relies on the availability and performance of antibodies that act on all proteoforms in an unbiased manner. Our prior work to charact  ...[more]

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