Recombinant Human Rac1 protein

**Background of Rac1 Recombinant Protein**

Rac1 (Ras-related C3 botulinum toxin substrate 1) is a small GTPase belonging to the Rho family, which plays a pivotal role in regulating cellular processes such as cytoskeletal reorganization, cell migration, proliferation, and adhesion. As a molecular switch, Rac1 cycles between an active GTP-bound state and an inactive GDP-bound state, mediated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Its activity is critical for signaling pathways that influence cell morphology, motility, and intracellular trafficking. Dysregulation of Rac1 is implicated in various diseases, including cancer metastasis, immune disorders, and neurodegenerative conditions.

Recombinant Rac1 protein is engineered through molecular cloning and expression in bacterial or eukaryotic systems (e.g., *E. coli* or mammalian cells), enabling large-scale production for research. The recombinant form often includes tags (e.g., His, GST, or FLAG) to facilitate purification and detection. Structural studies of Rac1 have revealed conserved domains involved in GTP/GDP binding and effector interactions, such as the Switch I and II regions. Mutant variants (e.g., constitutively active Rac1-G12V or dominant-negative Rac1-T17N) are widely used to dissect its signaling mechanisms.

Research applications of Rac1 recombinant protein include *in vitro* binding assays, enzymatic activity studies, and drug screening to identify modulators of Rac1 signaling. It is also employed in cell-based assays to investigate pathways like NADPH oxidase activation, lamellipodia formation, and epithelial-mesenchymal transition. Additionally, Rac1’s role in diseases has spurred interest in targeting it therapeutically, with studies exploring inhibitors to curb pathological signaling.

Overall, Rac1 recombinant protein serves as a vital tool for unraveling its biological functions and developing interventions for Rac1-associated disorders.