Recombinant Human E3 UFM1-protein ligase 1 (UFL1) fragment (residues 2-388) is a high-quality protein preparation ideal for studying ufmylation mechanisms and endoplasmic reticulum stress responses. This 387-amino acid fragment was carefully selected for optimal stability and solubility, making it perfect for structural studies, biochemical assays, and functional characterization of this crucial E3 ligase involved in multiple cellular processes.

E3 UFM1-protein ligase 1 (UFL1) is a key enzyme that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to target proteins. This essential E3 ligase plays critical roles in diverse cellular processes including ribosome recycling, DNA damage response, interferon signaling, and reticulophagy (ER-phagy). UFL1 catalyzes ufmylation of numerous substrates including CD274/PD-L1, DDRGK1, RPL26/uL24, and TP53/p53, thereby regulating immune checkpoint function, ribosome dissociation from ER membranes, and protein stability. The enzyme localizes primarily to the endoplasmic reticulum membrane but also functions in the cytoplasm, nucleus, and at chromosomal locations during DNA damage repair. UFL1-mediated ufmylation is particularly important during endoplasmic reticulum stress, where it promotes lysosomal degradation of ufmylated proteins and is essential for hematopoiesis, blood vessel development, and inflammatory responses.