Myocilin Protein, Human (HEK293, His)

Myocilin is a secreted glycoprotein that orchestrates the activation of diverse signaling pathways in neighboring cells, exerting control over various cellular processes such as cell adhesion, cytoskeleton organization, and cell migration. It plays a pivotal role in promoting substrate adhesion, spreading, and the formation of focal contacts, while concurrently exerting a negative regulatory influence on cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Myocilin also modulates the organization of the actin cytoskeleton by stimulating stress fiber formation, interacting with components of Wnt signaling pathways. Additionally, it facilitates cell migration through the activation of PTK2 and subsequent phosphatidylinositol 3-kinase signaling. Myocilin's impact extends to bone formation, where it dose-dependently promotes osteoblast differentiation via mitogen-activated protein kinase signaling, and it plays a crucial role in myelination within the peripheral nervous system through ERBB2/ERBB3 signaling. Moreover, Myocilin serves as a regulator of muscle hypertrophy through interactions with components of the dystrophin-associated protein complex and participates in the positive regulation of mitochondrial depolarization. It is implicated in neurite outgrowth and may contribute to the obstruction of fluid outflow in the trabecular meshwork. Myocilin forms homodimers, primarily via its N-terminus, and can assemble into higher-order oligomers. It engages in interactions with various proteins, including OLFM3, FN1, NRCAM, GLDN, NFASC, MYL2, SFRP1, FRZB, FZD7, FZD10, FZD1, WIF1, SNTA1, ERBB2, ERBB3, and SNCG, influencing diverse cellular functions and pathways.