Anti-REPS2 / RalBP1-associated Eps domain-containing protein 2

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. REPS2 antibody detects RalBP1-associated Eps domain-containing protein 2, a signaling adaptor that mediates endocytosis and receptor trafficking. The UniProt recommended name is RalBP1-associated Eps domain-containing protein 2 (REPS2). This cytoplasmic protein functions in clathrin-mediated endocytosis, growth factor receptor internalization, and signal transduction downstream of small GTPases such as RalA and RalB.Functionally, REPS2 antibody identifies a 639-amino-acid protein containing EH (Eps15 homology) domains that mediate interactions with endocytic machinery proteins including Eps15, RalBP1, and AP-2. REPS2 contributes to the internalization of epidermal growth factor receptor (EGFR) and other tyrosine kinase receptors, influencing receptor recycling and downregulation. It also participates in the regulation of cytoskeletal dynamics and cell adhesion through Ral GTPase-dependent pathways.The REPS2 gene is located on chromosome Xp22.3 and is expressed in epithelial tissues, neurons, and endocrine glands. In addition to its role in endocytosis, REPS2 modulates insulin signaling, exocytosis, and vesicular trafficking, providing a link between receptor activation and intracellular transport systems.Pathologically, aberrant REPS2 expression has been implicated in prostate cancer, breast cancer, and neurological disorders. Overexpression promotes cancer cell migration and survival by sustaining receptor tyrosine kinase signaling, while loss of REPS2 can impair receptor internalization and lead to altered growth factor responsiveness. Research using REPS2 antibody supports studies in membrane trafficking, cell signaling, and tumor progression.REPS2 antibody is validated for western blotting, immunofluorescence, and immunohistochemistry to detect endocytic adaptor proteins. NSJ Bioreagents provides REPS2 antibody reagents optimized for studies in receptor trafficking, cytoskeletal regulation, and cancer biology.Structurally, RalBP1-associated Eps domain-containing protein 2 contains N-terminal EH domains, central coiled-coil motifs, and proline-rich regions that mediate protein-protein interactions. These domains form scaffolds for complex assembly with signaling and endocytic components. This antibody enables the analysis of REPS2's role in receptor-mediated endocytosis and signaling modulation.