OMA1 Protein, Human (Cell-Free, His-SUMO)

Oma1 protein is an important metalloprotease in the inner mitochondrial membrane that is activated in response to stressors and cleaves targets such as OPA1, UQCC3, and DELE1. Under conditions of loss of membrane potential, Oma1 cleaves OPA1, thereby negatively regulating fusion. OMA1 Protein, Human (Cell-Free, His-SUMO) is the recombinant human-derived OMA1 protein, expressed by E. coli Cell-free , with N-His, N-SUMO labeled tag.

Oma1 Protein, classified as a metalloprotease, operates within the inner mitochondrial membrane as a crucial component of the quality control system. In response to diverse mitochondrial stressors, OMA1 becomes activated, leading to the proteolytic cleavage of specific target proteins, including OPA1, UQCC3, and DELE1. Under conditions causing a loss of mitochondrial membrane potential, OMA1 cleaves OPA1 at the S1 position, resulting in the inactivation of OPA1 and negative regulation of mitochondrial fusion. Moreover, OMA1 serves as a pivotal regulator of apoptosis, facilitating the remodeling of mitochondrial cristae through OPA1 cleavage upon BAK and BAX aggregation, thereby allowing the release of cytochrome c. In depolarized mitochondria, OMA1 may act as a backup protease for PINK1, mediating its cleavage and subsequent degradation by the proteasome. Additionally, OMA1 is implicated in the integrated stress response (ISR), cleaving DELE1 to generate the processed form (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI, initiating the ISR. OMA1's role in mitochondrial quality control extends to the regulation of lipid metabolism, maintenance of respiratory supercomplex stability, and adaptation to cold-stress conditions by influencing body temperature and energy expenditure. Its binding to cardiolipin suggests a potential role in regulating cardiolipin turnover.

Measured by its binding ability in a functional ELISA. Immobilized OMA1 at 5 μg/mL can bind human BZW2, the EC₅₀ of human BZM2 is 10.108-22.636 μg/mL.

Human

E. coli Cell-free

N-His;N-SUMO

Q96E52-1 (H14-S524)

115209  [NCBI]

HVFFRFNSLSNWRKCNTLASTSRGCHQVQVNHIVNKYQGLGVNQCDRWSFLPGNFHFYSTFNNKRTGGLSSTKSKEIWRITSKCTVWNDAFSRQLLIKEVTAVPSLSVLHPLSPASIRAIRNFHTSPRFQAAPVPLLLMILKPVQKLFAIIVGRGIRKWWQALPPNKKEVVKENIRKNKWKLFLGLSSFGLLFVVFYFTHLEVSPITGRSKLLLLGKEQFRLLSELEYEAWMEEFKNDMLTEKDARYLAVKEVLCHLIECNKDVPGISQINWVIHVVDSPIINAFVLPNGQMFVFTGFLNSVTDIHQLSFLLGHEIAHAVLGHAAEKAGMVHLLDFLGMIFLTMIWAICPRDSLALLCQWIQSKLQEYMFNRPYSRKLEAEADKIGLLLAAKACADIRASSVFWQQMEFVDSLHGQPKMPEWLSTHPSHGNRVEYLDRLIPQALKIREMCNCPPLSNPDPRLLFKLSTKHFLEESEKEDLNITKKQKMDTLPIQKQEQIPLTYIVEKRTGS

Approximately 74.7 kDa

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

Lyophilized powder

Lyophilized from a 0.2 μm solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.