• Enzymatically oxidize actin at methionine 44 & 47 (-actin nomenclature)
• Study the role of M44/47 oxidation on actin function

Enzymatic oxidation of actin at Met44/Met47 by the monooxygenase MICAL1 has been shown to destabilize F-actin in vivo and to play a key role in a growing number of cellular processes, including cytokinesis, axonal guidance, dendritic organization, synaptic development, heart and muscle development, and cell viability.

The Redox and CH domains of human MICAL1 protein have been produced and purified from a bacterial expression system;

• Protein tag: N-terminal His tag for purification
• UniProt ID: Q8TDZ2
• Redox & CH domains: aa 1-612
• Molecular weight: ~60 kDa
• Formulation: supplied as a lyophilized powder
• Composition: when resuspended to 1 mg/ml, the buffer composition is: 2 mM Tris pH 8.0, 20 mM NaCl, 1% sucrose, and 0.2% dextran

Protein purity is assessed by scanning densitometry of Coomassie Blue-stained protein on a 4-20% polyacrylamide gel. Purity is determined to be ≥90% pure.

The biological activity of MIC01 is determined by its ability to oxidize skeletal muscle actin AKL99 as determined by a subtilisin limited proteolysis assay (see datasheet). In this assay, MIC01 modifies ≥90% of the actin.