HTRA2 / OMI Antibody (C-Terminus)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
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Primary Accession | O43464 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 49kDa |
Dilution | IHC-P (5 µg/ml), WB (0.5-1 µg/ml), |
Gene ID | 27429 |
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Other Names | Serine protease HTRA2, mitochondrial, 3.4.21.108, High temperature requirement protein A2, HtrA2, Omi stress-regulated endoprotease, Serine protease 25, Serine proteinase OMI, HTRA2, OMI, PRSS25 |
Target/Specificity | peptide corresponding to 16 amino acids near the C-terminus of human Omi |
Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted. |
Precautions | HTRA2 / OMI Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | HTRA2 |
---|---|
Synonyms | OMI, PRSS25 |
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]: Ubiquitously expressed. |
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Background
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.
References
Faccio L.,et al.J. Biol. Chem. 275:2581-2588(2000).
Gray C.W.,et al.Eur. J. Biochem. 267:5699-5710(2000).
Faccio L.,et al.Genomics 68:343-347(2000).
Hillier L.W.,et al.Nature 434:724-731(2005).
Suzuki Y.,et al.Mol. Cell 8:613-621(2001).
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