Metalloendopeptidase OMA1 (human, recombinant)

OMA1 is an ATP-independent metalloproteinase encoded by OMA1. It is localized to the mitochondrial inner membrane and is comprised of a matrix-facing N-terminal domain, a transmembrane domain, and a C-terminal M48 metallopeptidase domain that is exposed to the intermembrane space. Under various stress conditions, including oxidative stress, heat stress, and mitochondrial membrane depolarization, OMA1 is activated and cleaves long isoforms of the GTPase optic atrophy 1 (OPA1) at the S1 cleavage site, leading to inhibition of mitochondrial fusion and increased mitochondrial fragmentation. Under stress conditions, OMA1 is also autocatalytically degraded, thereby limiting, and allowing for reversal of, the stress response. Oma1-/- mouse embryonic fibroblasts exhibit a loss of mitochondrial fragmentation upon exposure to hydrogen peroxide. Mice lacking Oma1 exhibit impaired thermogenesis, increased hepatic steatosis and serum triglyceride levels, and high-fat diet-induced obesity. Cayman's Metalloendopeptidase OMA1 (human, recombinant) can be used for Western blot and ELISA applications.Synonyms: Metalloprotease-related Protein 1, MPRP-1, OMA1, Overlapping with the m-AAA Protease 1 Homolog. Purity: >90%. Protein Identity Confirmed by Mass Spec: Yes. Source: Recombinant N-terminal His-tagged OMA1 expressed in E. coli. Amino Acids: 217-524. MW: 37.1 kDa. Formulation: (Request formulation change), 50 mM Tris, pH 8.0, with 150 mM sodium chloride, 10% glycerol, 0.5 M L-arginine, and 2 µM zinc chloride. UniProt Accession #: Q96E52.