UFL1 (F5P6L) Rabbit mAb recognizes endogenous levels of total UFL1 protein.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human UFL1 protein.

The ubiquitin-fold modifier 1 (UFM1) conjugation system (UFMylation) is a ubiquitin-like system that plays key roles in development and stress responses (1, reviewed in 2-4). Like ubiquitin, conjugation of UFM1 is a three-step enzymatic process involving a specific E1-activating enzyme (UBA5), an E2-conjugating enzyme (UFC1), and an E3-ligation enzyme (UFL1). Several substrates for UFMylation have been identified including DDRGK1, RPL26, p53, MRE11, histone H4, ASC1, CDK5RAP3, and CYB5R3 (5-12). Modification of these targets by UFM1 has direct effects on ER homeostasis, protein translation, and response to DNA damage. Notably, independent screens identified UFMylation as a key regulator of ER-phagy and autophagy (5,13,14). Aberrant UFMylation is associated with many pathological conditions, including cancer, diabetes, and inflammatory diseases (2-4).