UFL1 (Ubiquitin-fold modifier-conjugating enzyme 1) antibodies are specialized immunodetection tools targeting the E3 ligase central to the UFMylation pathway, a post-translational modification system critical for cellular processes like endoplasmic reticulum (ER) stress response, DNA repair, and immune regulation . These antibodies enable researchers to study UFL1’s roles in antiviral immunity, cancer biology, and protein homeostasis by detecting its expression, localization, and interaction partners across diverse experimental systems.
UFL1 stabilizes STING (stimulator of interferon genes), enhancing type I interferon production during DNA virus infections (e.g., HSV-1). Knockout studies in macrophages showed reduced IFN-β and increased viral replication .
Mechanistically, UFL1 deficiency accelerates K48-linked ubiquitination and proteasomal degradation of STING, independent of UFMylation .
UFL1 suppresses tumor immune evasion by promoting PD-L1 degradation via UFMylation. Reduced UFL1 expression correlates with poor anti-PD1 therapy response in melanoma and liver cancer .
In Ufl1-deficient mice, PD-L1 accumulates on cell surfaces, enhancing PD-1 binding and impairing CD8+ T-cell cytotoxicity .
UFL1 mitigates ER stress-induced apoptosis in bovine mammary epithelial cells by modulating autophagy markers (LC3, p62) and ROS levels .
LPS-induced granulosa cell apoptosis is alleviated by UFL1 via NF-κB pathway regulation .
Abcam ab226216: Detects a 90 kDa band in HeLa, HEK-293T, and Jurkat lysates . Validated in immunoprecipitation assays with minimal non-specific binding .
Proteintech 26087-1-AP: Identifies UFL1 in bovine mammary cells under ER stress, showing increased expression post-TM treatment .
Localizes UFL1 to mammary luminal cells and cytoplasm/nuclei of bovine mammary epithelial cells (BMECs) .
UFL1 antibodies will remain critical for exploring: