This study highlights Microscoop®’s ability to map the proteomic landscape of primary cilia at unprecedented resolution, identifying 4,233 proteins, including 524 known ciliary proteins critical for assembly, transportation, and signaling.
Microscoop® optoproteomics (combined localization and MS) reveals spatially resolved protein complexes such as spliceosomes and histone complexes, highlighting its potential to advance subcellular biology and uncover intricate cellular interactions.
Spatial proteomic discovery at specific subcellular locations often faces challenges due to limitations in current technology. Microscoop® spatial proteomics limitations by enabling hypothesis-free targeted protein identification within individual organelles, allowing exploration of subcellular protein interactions.
This study on stress granules (SG)s identified 1,754 consistently enriched proteins, with 74% of the top 50 ranked proteins being true positive SG proteins, underscoring Microscoop’s potential in advancing SG biology and driving therapeutic innovations.
Microscoop® identifies ciliary proteins with high specificity, uncovering critical insights into their structure and function, in a significant advancement in the exploration of ciliary biology and its implications for health and disease.
The Microscoop® identifies low-abundance proteins and overrepresented complexes in nuclear and nucleolar structures, such as the spliceosome and RNA polymerase, with remarkable specificity.