The Phospho-Rac1/Cdc42(Ser71) antibody is designed to detect Rac1 and Cdc42 proteins phosphorylated at serine 71. a post-translational modification linked to their functional regulation. Rac1 and Cdc42 belong to the Rho family of small GTPases, which act as molecular switches controlling cytoskeletal dynamics, cell motility, and intracellular signaling. Their activity is typically governed by GTP/GDP binding cycles, but phosphorylation has emerged as an alternative regulatory mechanism.
Phosphorylation at Ser71 in Rac1/Cdc42 is associated with altered interactions with downstream effectors or guanine nucleotide exchange factors (GEFs), potentially modulating their role in processes like cell migration, polarity, and vesicular trafficking. This modification has been implicated in pathological contexts, including cancer metastasis and neurological disorders, where aberrant Rac1/Cdc42 signaling contributes to disease progression.
The antibody is widely used in immunoblotting (Western blot), immunofluorescence, and immunoprecipitation to study the activation status and subcellular localization of phosphorylated Rac1/Cdc42 in response to stimuli such as growth factors, cytokines, or cellular stress. Researchers employ it to explore signaling pathways involving kinases like PAK1 or AKT, which may mediate Ser71 phosphorylation. Specificity is often validated using phosphorylation-blocking peptides or cells lacking Rac1/Cdc42 expression. Its applications span cancer biology, immunology, and neuroscience, offering insights into how post-translational modifications fine-tune GTPase activity in health and disease.