|Application ||WB, IHC-P, IF, E|
|Other Accession||AAB94569, 27429|
|Calculated MW||48841 Da|
|Application Notes||OMI antibody can be used for detection of OMI by Western blot at 0.5 to 1 μg/mL. Antibody can also be used for immunohistochemistry starting at 10 μg/mL. For immunofluorescence start at 20 μg/mL.|
|Other Names||OMI Antibody: OMI, PARK13, PRSS25, OMI, Serine protease HTRA2, mitochondrial, High temperature requirement protein A2, HtrA2, HtrA serine peptidase 2|
|Target/Specificity||OMI antibody was raised against a peptide corresponding to 15 amino acids near the N-terminus of human OMI.|
The immunogen is located within amino acids 120 - 170 of OMI.
|Reconstitution & Storage||OMI antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||OMI Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive.|
|Cellular Location||Mitochondrion intermembrane space. Mitochondrion membrane; Single-pass membrane protein. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID|
|Tissue Location||Isoform 1 is ubiquitous. Isoform 2 is expressed predominantly in the kidney, colon and thyroid|
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Provided below are standard protocols that you may find useful for product applications.
OMI Antibody: Inhibitor of apoptosis proteins (IAPs) were initially identified in baculoviruses as proteins that inhibit apoptosis of the host cells to allow time for viral replication. Cellular homologues containing at least one baculoviral IAP repeat (BIR) motif essential for their anti-apoptosis activity have been identified in yeasts and higher organisms and often act by binding and inhibiting processed caspases. The activity of these proteins can be modulated by the expression of proteins such as Smac/DIABLO and XAF-1 which displace or prevent the binding of caspases by IAPs. Recently, a mitochondrial serine protease termed Omi/HtrA2 has been found to bind IAPs. Similar to Smac, Omi possesses a conserved IAP-binding motif, but acts to cleave IAPs to irreversibly inactivate IAPs and promote apoptosis.
Crook NE, Clem RJ, and Miller LK. An apoptosis inhibiting baculovirus gene with a zinc finger like motif. J. Virol. 1993; 67:2168-2174.
Liston P, Fong WG, and Korneluk RG. The inhibitors of apoptosis: there is more to life than Bcl2. Oncogene 2003; 22:8568-80.
Vaux DL and Silke J. Mammalian mitochondrial IAP binding proteins. Biochem. Biophys. Res. Comm. 2003; 304:499-504.
Suzuki Y, Imai Y, Nakayama H, et al. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell 2001; 8:613-21.
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