E3 Ubiquitin-Protein Ligase AMFR (AMFR) Antibody

Background

E3 ubiquitin-protein ligase AMFR, also known as autocrine motility factor receptor (AMFR), is an enzyme that plays a crucial role in the ubiquitin-proteasome system (UPS), which is responsible for the targeted degradation of proteins within cells. AMFR functions as an E3 ubiquitin ligase, which means it catalyzes the transfer of ubiquitin molecules from E2 ubiquitin-conjugating enzymes to target proteins, marking them for degradation by the proteasome. This process, known as ubiquitination, is essential for regulating various cellular processes, including protein turnover, signal transduction, and the maintenance of protein homeostasis. AMFR has been implicated in other cellular functions: Regulation of protein trafficking: AMFR is involved in the quality control of membrane proteins, particularly those destined for degradation in the endoplasmic reticulum-associated degradation (ERAD) pathway. It helps target misfolded or unassembled membrane proteins for ubiquitination and subsequent degradation by the proteasome. Regulation of cellular signaling: AMFR has been shown to interact with and regulate various signaling molecules and pathways, including the epidermal growth factor receptor (EGFR) signaling pathway