UFC1 Antibody / Ubiquitin-fold modifier conjugating enzyme 1, 100ug

UFC1 antibody targets Ubiquitin-fold modifier conjugating enzyme 1, encoded by the UFC1 gene. Ubiquitin-fold modifier conjugating enzyme 1 is a cytoplasmic enzyme that functions as the E2 conjugating component of the UFM1 modification pathway, a ubiquitin-like system that regulates protein quality control and cellular stress responses. In this pathway, UFC1 accepts activated UFM1 from the E1 enzyme UBA5 and cooperates with the E3 ligase UFL1 to transfer UFM1 to specific substrate proteins, enabling ufmylation as a post-translational regulatory mechanism.<br><br>Functionally, Ubiquitin-fold modifier conjugating enzyme 1 plays an essential role in maintaining endoplasmic reticulum homeostasis and supporting cellular adaptation to proteotoxic stress. UFM1 conjugation mediated by UFC1 has been linked to ribosome-associated quality control, ER-associated protein processing, and regulation of secretory pathways. Through these activities, UFC1 helps coordinate cellular responses to disruptions in protein folding and trafficking. A UFC1 antibody supports studies examining ufmylation-dependent signaling and stress-regulated protein modification.<br><br>UFC1 is broadly expressed across many tissues and cell types, reflecting the fundamental requirement for UFM1-mediated regulation in diverse biological contexts. Its function is particularly relevant in cells with high secretory demand or elevated metabolic activity, where ER stress pathways must be precisely controlled. UFC1 operates within a dynamic enzyme complex, forming transient thioester-linked intermediates with UFM1 that enable controlled transfer to downstream targets.<br><br>From a disease-relevance perspective, dysregulation of the UFM1 conjugation system, including altered UFC1 activity, has been implicated in cancer, neurodevelopmental disorders, and inflammatory conditions. Impaired ufmylation can compromise ER integrity and protein homeostasis, contributing to pathological cellular states. As a result, Ubiquitin-fold modifier conjugating enzyme 1 has emerged as a protein of interest in studies of stress signaling and disease-associated protein modification pathways.<br><br>At the molecular level, UFC1 contains conserved catalytic residues characteristic of E2 enzymes that are required for UFM1 thioester bond formation. Its apparent behavior in biochemical assays can be influenced by interaction partners, enzymatic state, or cellular context. UFC1 antibody reagents support research applications focused on ufmylation biology, ER stress regulation, and protein quality control, with NSJ Bioreagents providing reagents intended for research use.

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