ARRB1 (β-arrestin-1) is a ubiquitously expressed intracellular scaffolding protein belonging to the arrestin family. It plays a critical role in regulating G protein-coupled receptor (GPCR) signaling by mediating receptor desensitization, internalization, and downstream signaling cascades. Beyond GPCR modulation, ARRB1 interacts with diverse signaling molecules (e.g., MAPK, AKT) and participates in non-GPCR pathways, including Wnt/β-catenin and NF-κB, influencing cell proliferation, migration, and apoptosis. Its dynamic subcellular shuttling between the cytoplasm and nucleus allows transcriptional regulation. Dysregulation of ARRB1 is implicated in cancer, neurological disorders, and metabolic diseases.
ARRB1 antibodies are essential tools for studying these processes. They enable detection of endogenous ARRB1 expression, post-translational modifications (e.g., phosphorylation), and protein-protein interactions via techniques like Western blotting, immunoprecipitation, and immunofluorescence. Specific antibodies can distinguish ARRB1 from its homolog ARRB2 (β-arrestin-2) despite ~78% amino acid similarity. Validation includes testing in knockout cell lines or tissues to confirm specificity. Commercially available ARRB1 antibodies are typically raised against epitopes in the N- or C-terminal regions. Researchers use these antibodies to explore ARRB1's roles in disease mechanisms, drug response, and therapeutic targeting, particularly in contexts involving GPCR dysregulation or aberrant signal transduction.