MICAL2 Protein, Human (P.pastoris, His)

The MICAL2 protein is a methionine monooxygenase that crucially promotes F-actin depolymerization by oxidizing actin residues "Met-44" and "Met-47" to form methionine sulfoxide. This modification prevents actin filaments from repolymerizing. MICAL2 Protein, Human (P.pastoris, His) is the recombinant human-derived MICAL2 protein, expressed by P. pastoris , with N-His labeled tag.

MICAL2, a methionine monooxygenase, plays a crucial role in promoting the depolymerization of F-actin by mediating the oxidation of residues 'Met-44' and 'Met-47' on actin, resulting in the formation of methionine-sulfoxide. This oxidative modification leads to actin filament disassembly, preventing repolymerization. Additionally, MICAL2 regulates the disassembly of branched actin networks by oxidizing ARP3B-containing ARP2/3 complexes, ultimately causing ARP3B dissociation from the network. Furthermore, MICAL2 serves as a key regulator in the SRF signaling pathway induced by nerve growth factor and serum. It mediates the oxidation and subsequent depolymerization of nuclear actin, enhancing the presence of MKL1/MRTF-A in the nucleus and facilitating SRF:MKL1/MRTF-A-dependent gene transcription. Notably, MICAL2 does not activate the SRF:MKL1/MRTF-A pathway through RhoA.

Human

P. pastoris

N-His

O94851 (1M-495H)

9645  [NCBI]

MGENEDEKQAQAGQVFENFVQASTCKGTLQAFNILTRHLDLDPLDHRNFYSKLKSKVTTWKAKALWYKLDKRGSHKEYKRGKSCTNTKCLIVGGGPCGLRTAIELAYLGAKVVVVEKRDSFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVKVLEPPEDQENQKIGWRAEFLPTDHSLSEFEFDVIIGADGRRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDCTHYFVMTAKKQSLLDKGVIINDYIDTEMLLCAENVNQDNLLSYAREAADFATNYQLPSLDFAMNHYGQPDVAMFDFTCMYASENAALVRERQAHQLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMVKSWNQGTPPLELLAERESLYRLLPQTTPENINKNFEQYTLDPGTRYPNLNSHCVRPHQVKHLYITKELEH

Approximately 58.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.