Recombinant Human EPS8 Protein

Epidermal growth factor receptor pathway substrate 8 (EPS8) is a multifunctional protein involved in regulating actin cytoskeleton dynamics, receptor signaling, and vesicular trafficking. Initially identified as a substrate of the epidermal growth factor receptor (EGFR), EPS8 interacts with signaling molecules like Rac and Rab5. influencing cellular processes such as migration, endocytosis, and membrane remodeling. Its modular structure, comprising a PTB domain, SH3-binding motifs, and an actin-binding region, enables diverse protein interactions. Dysregulation of EPS8 is linked to cancer progression, neurological disorders, and immune dysfunction, with overexpression observed in tumors, correlating with metastasis and poor prognosis.

Recombinant human EPS8 (rhEPS8) is produced via heterologous expression systems (e.g., E. coli or mammalian cells) for functional studies and therapeutic exploration. Purified rhEPS8 facilitates in vitro analyses of its molecular mechanisms, including actin capping/bundling activities and pathway modulation. Researchers utilize it to probe EPS8’s role in EGFR-mediated signaling cascades, neuronal development, or immune cell activation. Recent studies highlight its potential as a biomarker or therapeutic target, particularly in cancers reliant on EGFR or cytoskeletal dysregulation. rhEPS8 also aids drug discovery by enabling high-throughput screening for inhibitors disrupting EPS8-associated oncogenic networks. Its applications extend to structural biology, helping resolve atomic-level interactions critical for rational drug design.