UBQLN1 (ubiquilin-1) is a member of the ubiquitin-like protein family, primarily involved in regulating protein degradation pathways, including the ubiquitin-proteasome system and autophagy. It acts as a molecular chaperone, facilitating the recognition and transport of polyubiquitinated substrates to proteasomes for degradation. UBQLN1 contains an N-terminal ubiquitin-like (UBL) domain for proteasomal interaction and a C-terminal ubiquitin-associated (UBA) domain for binding ubiquitinated targets, enabling its critical role in maintaining protein homeostasis. Dysregulation of UBQLN1 has been linked to neurodegenerative diseases, such as Alzheimer’s and Parkinson’s, where protein aggregation is a hallmark.
Antibodies targeting UBQLN1 are essential tools for studying its expression, localization, and function in cellular and disease models. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to detect UBQLN1 levels in tissues or cultured cells. Such antibodies help investigate UBQLN1's involvement in stress responses, DNA repair, and autophagy-lysosomal pathways. Commercial UBQLN1 antibodies are typically raised in hosts like rabbits or mice, validated for specificity against conserved epitopes across species. Researchers also utilize these antibodies to explore UBQLN1's interactions with disease-associated proteins, such as amyloid-β or tau, providing insights into its potential therapeutic or diagnostic relevance in neurodegeneration and cancer.