This protein kinase is a central regulator of the actin cytoskeleton and cell polarity, influencing numerous cellular processes. It is critical for smooth muscle contraction, stress fiber and focal adhesion formation, actin organization, neurite retraction, and cell motility. Through phosphorylation of various substrates, including ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A, and VIM, it governs key structural and signaling pathways. It also phosphorylates SORL1 and IRF4, extending its role to diverse biological functions.
This kinase acts as a negative regulator of VEGF-induced angiogenesis in endothelial cells and positively modulates p42/MAPK1-p44/MAPK3 and p90RSK/RPS6KA1 activation during myogenic differentiation. It is crucial for the timely initiation of centrosome duplication and inhibits keratinocyte terminal differentiation.
It may regulate actomyosin bundle organization for eyelid and ventral body wall closure and is vital for maintaining spine and synaptic properties in the hippocampus. Additionally, it contributes to circadian rhythms in vascular contractility and myofilament calcium sensitivity in the aorta by modulating myosin light chain phosphorylation. These roles emphasize its significance in cytoskeletal dynamics, differentiation, and physiological processes.
| Product Name | Recombinant Human ROCK2 Protein |
| Accession | O75116 |
| Host Species | Human |
| Gene | ROCK2 |
| Source | Sf9 (Baculovirus infected) |
