Metalloendopeptidase OMA1 (human, recombinant)

OMA1 is an ATP-independent metalloproteinase encoded by OMA1.¹ 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.^1,2 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.^1,2,3 Under stress conditions, OMA1 is also autocatalytically degraded, thereby limiting, and allowing for reversal of, the stress response.^2,3 Oma1^-/- mouse embryonic fibroblasts exhibit a loss of mitochondrial fragmentation upon exposure to hydrogen peroxide.² Mice lacking Oma1 exhibit impaired thermogenesis, increased hepatic steatosis and serum triglyceride levels, and high-fat diet-induced obesity.⁴ Cayman’s Metalloendopeptidase OMA1 (human, recombinant) can be used for Western blot and ELISA applications.

WARNING This product is not for human or veterinary use.

1. Levytskyy, R.M., Bohovych, I., and Khalimonchuk, O. Metalloproteases of the inner mitochondrial membrane. Biochemistry 56(36), 4737-4746 (2017).

2. Baker, M.J., Lampe, P.A., Stojanovski, D., et al. Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics. EMBO J. 33(6), 578-593 (2014).

3. Quirós, P.M., Langer, T., and López-Otín, C. New roles for mitochondrial proteases in health, ageing and disease. Nat. Rev. Mol. Cell Biol. 16(6), 345-359 (2015).

4. Quirós, P.M., Ramsay, A.J., Sala, D., et al. Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice. EMBO J. 31(9), 2117-2133 (2012).