The DUSP12 antibody is a crucial tool for studying the dual-specificity phosphatase 12 (DUSP12), a member of the protein tyrosine phosphatase (PTP) family. DUSP12. also known as YVH1. is a non-classical dual-specificity phosphatase that regulates mitogen-activated protein kinase (MAPK) signaling pathways by dephosphorylating both tyrosine and serine/threonine residues. Unlike other DUSPs, DUSP12 lacks a MAPK-binding domain but contains a unique N-terminal domain and a conserved C-terminal catalytic phosphatase domain, suggesting distinct regulatory mechanisms. It is implicated in diverse cellular processes, including cell cycle progression, stress responses, and RNA metabolism, with potential roles in cancer, neurodegeneration, and metabolic disorders.
DUSP12 antibodies are widely used in techniques like Western blotting, immunoprecipitation, and immunohistochemistry to detect protein expression, localization, and interactions. These antibodies help elucidate DUSP12’s tissue-specific _expression (e.g., high levels in liver, kidney, and heart) and its dynamic regulation under physiological or pathological conditions. Research has linked DUSP12 to tumor suppression, viral infection responses, and glucose homeostasis, though its precise mechanisms remain under investigation. Validated antibodies with high specificity are essential, as cross-reactivity with other DUSP family members may complicate interpretation. Overall, DUSP12 antibodies serve as vital reagents for unraveling the enzyme’s functional roles and therapeutic potential.