HTRA2/OMI Protein, Human (His)

HTRA2/OMI, a serine protease, crucially induces cell death via multiple mechanisms.It directly inhibits BIRC proteins, intensifying caspase activity, and can also induce cell death through a BIRC-independent, caspase-independent pathway, relying on its serine protease activity.Additionally, during apoptosis, it cleaves THAP5, promoting its degradation.Notably, isoform 2 lacks apparent proteolytic activity.HTRA2/OMI Protein, Human (His) is the recombinant human-derived HTRA2/OMI protein, expressed by E.coli , with C-His labeled tag.

HTRA2/OMI, a serine protease, exhibits proteolytic activity against a non-specific substrate, beta-casein. It plays a pivotal role in cell death induction through multiple mechanisms. One mechanism involves direct binding to and inhibition of BIRC proteins (inhibitor of apoptosis proteins, IAPs), leading to heightened caspase activity. Alternatively, HTRA2/OMI can induce cell death through a BIRC inhibition-independent, caspase-independent pathway, relying on its serine protease activity. Furthermore, during apoptosis, it cleaves THAP5, promoting its degradation. Notably, isoform 2 appears to lack proteolytic activity.

Protease activity demonstrated by HtrA2 cleavage of bovine β-casein. Incubation of β-casein at 0.2 mg/mL with HTRA2/OMI Protein, Human (His) at 0.02 mg/mL (ratio of 10:1) for 60 minutes at 45°C in 50 mM Tris, pH 8.0, which results in >95% cleavage of β-casein, as revealed by SDS-PAGE.

Human

E. coli

C-His

O43464 (A134-E458)

27429  [NCBI]

Approximately 36.5 kDa

Greater than 87% as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.2 μm filtered solution of 50 mM Tris, 0.3M NaCl, 1 mM DTT, 20% Glycerol, pH 7.8.

<1 EU/μg, determined by LAL method.

N/A.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.