|Application ||WB, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||48841 Da|
|Other Names||HTRA2 , HtrA2 , PARK13 , OMI , PRSS25|
|Format||100 µg (0.5 mg/ml) antigen affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 50% glycerol, 1% BSA, and 0.02% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Precautions||HtrA2/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.
Human HtrA2 (also designated Omi) is a novel member of the HtrA serine protease family and is highly homologous to HtrA (also known as L56 and HtrA1). HtrA2 is ubiquitously expressed nuclear protease that is capable of autoproteolysis. The HtrA2 protein exists as two polypeptides of 38 and 40 kDa and as an alternatively spliced form called D-Omi, which is predominately expressed in the kidney, colon and thyroid. Like HtrA, HtrA2 is involved in the degradation aberrantly folded proteins during conditions of cellular stress, s µggesting that it may possess a chaperone-like role under normal conditions.
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