cAPX Antibodies

Target Information

cAPX encodes a cytosolic class I heme-dependent ascorbate peroxidase that localizes predominantly to the cytosol, where it functions as a major enzymatic sink for hydrogen peroxide generated during normal metabolism and during oxidative, light, and abiotic/biotic stress responses. The canonical cAPX protein is a soluble ~250 amino acid monomeric polypeptide of the plant ascorbate peroxidase family that binds one noncovalently associated heme cofactor per subunit and adopts a predominantly alpha-helical peroxidase fold closely related to cytochrome c peroxidase; structural studies show assembly as a noncovalent homodimer in solution/crystals, with a conserved proximal histidine heme ligand and other conserved residues required for peroxide turnover and radical chemistry. Functionally, cAPX catalyzes the reduction of H2O2 to water using L-ascorbate as the preferred electron donor, thereby limiting ROS-mediated macromolecular damage while shaping H2O2-dependent signaling outputs; consistent with this role, genetic and physiological studies support cAPX as a central component of cellular redox homeostasis and stress acclimation, with loss or suppression of cAPX lowering detoxification capacity and promoting H2O2 accumulation during stress-associated processes.

Synonyms

ASCORBATE PEROXIDASE; ascorbate peroxidase 1; ATAPX01; ATAPX1; CS1; F24B9.2; F24B9_2; maternal effect embryo arrest 6; MEE6