The RNF5 antibody is a crucial tool for studying the Ring Finger Protein 5 (RNF5), an E3 ubiquitin ligase involved in the ubiquitin-proteasome system. RNF5. also known as RMA1. plays a key role in endoplasmic reticulum-associated degradation (ERAD), targeting misfolded or damaged proteins for proteasomal degradation. It contains a conserved RING domain critical for its ligase activity and is localized to the endoplasmic reticulum (ER) and mitochondria-associated membranes (MAMs), where it regulates stress responses, protein quality control, and cellular homeostasis. RNF5 substrates include proteins like HSP70. CFTR, and PDIA3. linking it to diseases such as cystic fibrosis, cancer, and neurodegenerative disorders.
Antibodies against RNF5 are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to assess its expression, subcellular localization, and interactions. Research highlights RNF5's dual roles in cancer—acting as both a tumor suppressor (by degrading oncoproteins) and promoter (via modulating metastasis-related pathways). It also influences mitochondrial dynamics and autophagy, connecting it to Parkinson’s and Alzheimer’s diseases.
The development of specific RNF5 antibodies has advanced studies on ER stress, unfolded protein response, and therapeutic targeting of protein degradation pathways. Validated antibodies are essential for elucidating RNF5's regulatory mechanisms and its potential as a biomarker or therapeutic target in diverse pathologies.