Ubiquitin binding proteins, also known as ubiquitin receptors, are important components of both the ubiquitin-proteasome system (UPS) and the autophagy-lysosome pathway. These proteins recognize and interact with ubiquitin chains on target substrates, thereby facilitating their degradation or directing them towards specific cellular processes. For example, p62/SQSTM1 is a ubiquitin receptor that plays a critical role in selective autophagy. It contains both a ubiquitin-binding domain and a LC3-interacting region (LIR), allowing it to bridge ubiquitylated cargo to autophagic membranes. P62 targets various substrates, including misfolded proteins and damaged organelles, for degradation through autophagy. For instance, when mitochondria are damaged, they are ubiquitylated, with p62 recognizing these ubiquitin tags and delivering the damaged mitochondria to autophagosomes for clearance in a process known as mitophagy. Rad23 is a ubiquitin receptor that plays a role in the proteasomal degradation pathway. It acts as a shuttle, facilitating the delivery of ubiquitylated substrates to the 26S proteasome. Rad23 binds to both ubiquitin chains and the proteasomal subunit Rpn1, thereby aiding in substrate recognition and degradation. One of its substrates is the cyclin-dependent kinase inhibitor p27, which is targeted for proteasomal degradation through Rad23-mediated recognition. Dsk2 (Daughter of sevenless 2), like Rad23, is another ubiquitin receptor involved in delivering ubiquitylated proteins to the proteasome. It contains a ubiquitin-like (UBL) domain that binds to ubiquitin and a ubiquitin-associated (UBA) domain that interacts with proteasomal subunits. Dsk2 recognizes polyubiquitylated substrates and facilitates their proteasomal degradation. For example, it participates in the degradation of misfolded or damaged proteins to maintain protein quality control. NBR1 (Neighbour of BRCA1 gene 1) is another ubiquitin receptor involved in selective autophagy. It contains a ubiquitin-binding domain and a LIR, allowing it to link ubiquitylated cargo to autophagic membranes. NBR1 plays a role in the clearance of various substrates, including protein aggregates and damaged organelles, by directing them to autophagosomes for degradation. In Parkinson's disease, NBR1 is implicated in the removal of aggregates containing α-synuclein, a hallmark of the disease. Optineurin (OPTN) is a ubiquitin receptor associated with several cellular processes, including autophagy and inflammation. It contains a ubiquitin-binding domain and an LC3-binding domain, enabling it to mediate the autophagic clearance of ubiquitylated cargo. OPTN is involved in the removal of damaged mitochondria via mitophagy and regulates NF-κB signaling by binding to ubiquitylated components of the pathway. Mutations in OPTN are linked to certain forms of amyotrophic lateral sclerosis (ALS). UBD (Ubiquitin-binding domain)-containing proteins like UBQLN1, contain ubiquitin-binding domains and play roles in protein quality control. UBQLN1 is involved in shuttling ubiquitylated proteins to the proteasome, contributing to the degradation of misfolded or damaged proteins. It is also implicated in neurodegenerative diseases like Alzheimer's, where it associates with protein aggregates. Finally, Rpn10 (Regulatory Particle non-ATPase 10) is a ubiquitin receptor within the proteasomal regulatory particle. It recognizes and binds to ubiquitylated substrates, facilitating their engagement with the proteasome. This interaction is critical for the efficient degradation of ubiquitylated proteins by the proteasome. We provide a wide product catalogue of research reagents for studying ubiquitin binding proteins, including RAP80 antibodies. Explore our full ubiquitin binding proteins product range below and discover more, for less.