TRAIP (TRAF-interacting protein) is a conserved eukaryotic protein involved in genome stability, DNA repair, and cell cycle regulation. Initially identified through its interaction with TNF receptor-associated factors (TRAFs), TRAIP functions as an E3 ubiquitin ligase, playing critical roles in replication stress response, ribosome biogenesis, and mitotic progression. Structurally, it contains a RING domain for ubiquitination activity, coiled-coil regions for protein interactions, and a nucleolar localization signal.
TRAIP is essential for resolving stalled replication forks by promoting the removal of replication barriers and activating the ATR/CHK1 checkpoint. It also participates in 5S rRNA processing and ribosome assembly. Mutations in TRAIP are linked to human diseases, including 3M syndrome (characterized by growth retardation) and microcephalic primordial dwarfism. In cancer, TRAIP dysregulation correlates with genomic instability and tumor progression, making it a potential therapeutic target.
Antibodies targeting TRAIP are vital tools for studying its expression, localization, and molecular interactions. They are used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to explore TRAIP’s roles in DNA damage response, cell cycle checkpoints, and disease mechanisms. These antibodies also aid in identifying TRAIP-associated pathways in cancer models and developmental disorders, providing insights into its dual functions in homeostasis and disease.