This ADC product is comprised of an anti-MUC16 monoclonal antibody (clone 3A5) conjugated via a BMPEO linker to DM1. The DM1 is targeted to certain cancers by immunerecognition and delivered into cancer cells via receptor mediated endocytosis. Within the cell, DM1 binds to tubulins, interrupts microtubule dynamics, and subsequently, induces cell death.
ADC Target
- Target Entrez Gene ID
- 94025
- Overview
- MUC16 is a Protein Coding gene. Diseases associated with MUC16 include mucinous ovarian cystadenoma and pleural cancer. Among its related pathways are Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein and Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
ADC Antibody
- Overview
- Anti-MUC16 antibody, clone # 3A5
ADC Linker
- Name
- BMPEO (bis-maleimido-trioxyethylene glycol)
- Description
- Noncleavable linkers, is considered noncleavable-meaning linker cleavage, and payload release does not depend on the differential properties between the plasma and some cytoplasmic compartments. Instead, the release of the cytotoxic drug is postulated to occur after internalization of the ADC via antigen-mediated endocytosis and delivery to lysosomal compartment, where the antibody is degraded to the level of amino acids through intracellular proteolytic degradation.
ADC payload drug
- Name
- DM1 (N2’-Deacetyl-N2’-(3-mercapto-1-oxopropyl)maytansine)
- Description
- Derived from Maytansinoid,a group of cytotoxins structurally similar to rifamycin, geldanamycin, and ansatrienin. The eponymous natural cytotoxic agent maytansine is a 19-member lactam (ansa
macrolide) structure originally isolated from the Ethiopian shrub Maytenus ovatus. Maytansinoids can bind to tubulin at or near the vinblastine-binding site, which interfere the formation of microtubules and depolymerize already formed microtubules, inducing mitotic arrest in the intoxicated cells.
For Research Use Only. NOT FOR CLINICAL USE.
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