Rejuvenated vintage tissue sections highlight individual antigen fate during processing and long term storage.
Antigen-bearing proteins become progressively unavailable to immunodetection after prolonged storage of routine sections, exposed to a variety of agents, such as moisture, oxygen and temperature. By proteomic analysis, the antigens are retained in the sections and definitely in the tissue block, pointing to fixation-independent, storage time-dependent protein modifications. Based on previous experience, we hypothesized that a combined exposure to a reducing agent and to chemicals favouring protein conformation changes would reverse the masking in aged sections. Disaccharides, lactose and sucrose, and a surfactant, added to a standard antigen retrieval buffer, reverse the negative changes in aged sections. Furthermore, they provide enhanced access to antigens in freshly cut sections, but not universally, revealing additional factors, besides heat and calcium chelation, required for antigen retrieval of individual proteins. This dataset contains supplementary data to the manuscript, raw data and analytical tools.
Additional Metadata for University of Milano - Bicocca
|ERC Keywords||LS1_9 Structural biology and its methodologies (e.g. crystallography, cryo-EM, NMR and new technologies), LS2_9 Proteomics, LS7_3 Other medical technologies for diagnosis and monitoring of diseases, LS9_2 Applied bioengineering, synthetic biology, chemical biology, nanobiotechnology, metabolic engineering, protein and glyco-engineering, tissue engineering, biocatalysis, biomimetics|
|SSD Classification||MED/08 - ANATOMIA PATOLOGICA, MED/04 - PATOLOGIA GENERALE, BIO/12 - BIOCHIMICA CLINICA E BIOLOGIA MOLECOLARE CLINICA|
|Grant||IMMUN-HUB - Sviluppo di nuove molecole di seconda generazione per immunoterapia oncologica (2019-NAZ-0120)|