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Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Additionally we are shipping MICAL2 Proteins (3) and many more products for this protein.
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Data suggest that MICAL2 protein might be an important regulator of epithelial to mesenchymal transition and therefore a promising target for anti-metastatic therapy.
These data show that SRF/MRTF-A signaling is regulated by MICAL-2-dependent redox regulation of nuclear actin.
although MICAL1 is auto-inhibited by its C-terminal coiled-coil region, MICAL2 remains constitutively active and affects stress fibers, suggesting differential but complementary roles for MICAL1 and MICAL2 in actin microfilament regulation
MICAL2-PV is likely to be involved in cancer progression of prostate cancer and could be a candidate as a novel molecular marker and/or target for treatment of prostate cancers.
show that this strategy is used by MICAL-2. Thus, our data suggest that MICAL-2 could regulate catalysis through the monooxygenase domain alone
Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (By similarity).
flavoprotein oxidoreductase MICAL2
, microtubule associated monoxygenase, calponin and LIM domain containing 2
, molecule interacting with CasL protein 2
, protein MICAL-2
, protein-methionine sulfoxide oxidase MICAL2