Marcel Raspe Email & Phone Number

Westerduinweg 3, Petten, The Netherlands

Managing the daily affairs and projectmanagement for an ISO17025 (L621) accredited radiochemical laboratorium

Westerduinweg 3, 1755Le Petten, The Netherlands

Westerduinweg 3, 1755 Le, Petten

Consultancy and Project Management for Nuclear Waste and Decommissioning

Westerduinweg 3, 1755 Le Petten

As an Analytical Chemist, I assisted in the HEU to LEU target conversion of the Petten (NL) Mo-99 production.Tasks are:Writing and evaluating SOPs, Validation Protocols and Reports according to GMP and ICH/FDA guidelinesAssisting with analytical chemical assaysData analysis

Amsterdam, Netherlands

Research: - Oncology - Epigenetics and Ubiquitin conjugation and deconjugation. - Operating and maintaining the Frequency-domain Fluorescence Lifetime Imaging MicroscopeFrequently performed assays and skills are: - fluorescence (confocal) microscopy - fluorescence lifetime imaging (Time-domain & Frequency-domain) - Western-blotting - Cell Culture - Experience with designing and implementing a siRNA DUB screen

Amsterdam, The Netherlands

Finished a thesis entiteld "Tripeptidyl Peptidase II in antigen processing and neurodegenerative diseases"Scientific background: - Neurodegenerative diseases such as Alzheimer and Huntington's dieases - Immunity (MHC class I loading)Frequently performed assays and skills were: - Western-blotting- Confocal Microscopy- Cell Culture- Protein Degradation Assays (with internally quenched peptides)- Micro-injection of cells- Molecular Cloning- I supervised several bachelor and master studentsSummary of the thesis: In cells, new proteins are continuously produced and the majority of old, obsolete or misfolded proteins are rapidly degraded by the proteasome complex. The proteasome degrades these proteins into multiple proteolytic fragments, named peptides. These peptides are further degraded into single amino-acids by a large family op peptidases. A small fraction of these peptides escape complete degradation, are trimmed to the correct size by peptidases, and are subsequently transported to the cell-membrane. At the membrane, immune-cells determine if these peptides originate from endogenous or from viral proteins. In my thesis we describe the substrate specificity of several peptidases. Moreover we designed several substrates and inhibitors for Tripeptidyl Peptidase II. In many neurodegenerative diseases, aggregates of proteins and proteolytic fragments are identified in neuronal cells, suggesting improper degradation. Huntington’s disease, for example, is a well-known disease that is characterized by an expanded polyGlutamine tract. The neurons of Huntington’s patients contain frequently aggregates of these polyGlutamine rich fragments. We identified two peptidases that can degrade these expanded polyGlutamine repeats and we established that polyGlutamine peptides by itself are sufficient to initiate aggregation in-vivo.

Master'S Degree, Biochemistry

Activities and Societies: ASV Hendrik De Chemische Binding

Secondary School Diploma, Dutch, English, Math (A&B), Physics, Chemistry, Economics, History