Ubiquitin specific peptidase 20 (USP20) is an enzyme that is responsible for removing ubiquitin from ubiquitin-labeled proteins, thereby stabilizing the protein and preventing its degradation through the proteasome. USP20 is involved in regulating many signaling pathways including cell proliferation, migration, tumor growth, and glucose metabolism. These UCF mice posses loxP sites flanking exons 7-8 of the Usp20 gene. Mice that are homozygous for this floxed allele are viable and fertile. When bred to mice that express tissue-specific Cre recombinase, resulting offspring will have exons 7-8 deleted in the cre-expressing tissues. The donating laboratory bred these UCF mice to a Myh6-Cre mouse line, on a C57BL/6J background, and confirmed complete loss of USP20 in heart tissue resulting in significant LV dysfunction with pressure overload as observed in USP20 genetrap KO mice (<a href="https://pubmed.ncbi.nlm.nih.gov/39365672/">PMID:39365672</a>). These UCF mice may be useful when studying the pathogenesis of neurodegenerative diseases, cardiac injury, atherosclerosis and tumorigenesis.

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UCF mice possess loxP sites flanking exons 7-8 of the Usp20 gene. These mice may be useful for studying the deubiquitinase activity of USP20 in tumorigenesis, metabolic disorders, and neurological diseases.

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