Anti-Human UFM1 Antibody Pair

Product Description: Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein that plays a crucial role in various cellular processes through a post-translational modification known as UFMylation. This process involves the covalent attachment of UFM1 to lysine residues on target proteins, similar to ubiquitination. UFM1 is essential for maintaining cellular homeostasis, particularly in the endoplasmic reticulum (ER), where it regulates ER-associated degradation, ribosome quality control, and responses to stress. Mutations in genes associated with the UFM1 system, such as UFM1 itself, UBA5, and UFC1, have been linked to severe human diseases, including hereditary developmental epileptic encephalopathy and Schohat-type osteochondrodysplasia. These conditions underscore the importance of UFM1 in developmental processes and highlight its potential as a therapeutic target in diseases related to protein misfolding and stress responses in cells. Protein Function: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776, PubMed:30626644, PubMed:38377992, PubMed:38383785). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776). Ufmylation is involved in various processes, such as ribosome recycling, response to DNA damage, transcription or reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:25219498, PubMed:32160526, PubMed:38383785) [The Uniprot Consortium]