Recombinant Human RhoG protein

RhoG (Ras homolog family member G) is a small GTP-binding protein belonging to the Rho GTPase family, which plays a central role in regulating cytoskeletal dynamics, cell migration, and membrane trafficking. Discovered in the 1990s, RhoG shares structural and functional similarities with other Rho family members like Rac1 and Cdc42. operating as a molecular switch by cycling between active GTP-bound and inactive GDP-bound states. Its activity is tightly regulated by guanine nucleotide exchange factors (GEFs), GTPase-activating proteins (GAPs), and guanine nucleotide dissociation inhibitors (GDIs). RhoG is notably involved in signaling pathways that control cell adhesion, neurite outgrowth, and phagocytosis, often interacting with downstream effectors such as ELMO and Dock180 to activate Rac1. thereby linking RhoG to broader cellular processes.

Recombinant RhoG proteins are engineered using heterologous expression systems (e.g., E. coli or mammalian cells) to produce purified, functional proteins for research. These tools enable studies on RhoG’s structure-function relationships, activation mechanisms, and interactions with regulatory molecules. Recombinant RhoG is particularly valuable in dissecting pathways implicated in cancer metastasis, immune cell migration, and neurological disorders, where dysregulated Rho GTPase signaling is frequently observed. For example, aberrant RhoG expression has been linked to invasive tumor behavior and impaired neuronal development. Additionally, recombinant RhoG serves as a critical reagent in drug discovery, aiding the identification of inhibitors or activators targeting Rho GTPase-related pathologies. Its applications extend to in vitro assays, structural studies (e.g., crystallography), and cellular models to explore RhoG’s role in health and disease.