Recombinant Human HtrA2 / Omi protein (His tag)
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Recombinant Human HtrA2 / Omi protein (His tag) is a Human Fragment protein, in the 133 to 358 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
OMI, PRSS25, HTRA2, High temperature requirement protein A2, Omi stress-regulated endoprotease, Serine protease 25, Serine proteinase OMI, HtrA2
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human HtrA2 / Omi protein (His tag) (AB217833)
SDS-PAGE analysis of ab217833.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The degradation and signaling processes of HtrA2/Omi protect against proteotoxic stress. It operates within the mitochondria and under stress conditions relocates to the cytosol where it can influence apoptosis. HtrA2/Omi can interact with inhibitors of apoptosis proteins (IAPs) and by doing this promotes apoptosis when necessary. This regulation of cell death links HtrA2/Omi to the cellular quality control mechanisms directly impacting cell survival and health.
Pathways
HtrA2/Omi integrates into the mitochondrial apoptosis pathway and is important in Parkinson's disease pathways. Through its interactions with apoptosis regulators like XIAP HtrA2/Omi facilitates the removal of unwanted cells. Additionally it participates in signaling pathways involving caspases and other pro-apoptotic factors. Its activity ensures proper communication and response within these pathways to maintain cellular balance and respond to stressors or damage.
Specifications
Form
Liquid
General info
Function
Isoform 1. Serine protease that shows proteolytic activity against a non-specific substrate beta-casein (PubMed : 10873535). Promotes apoptosis by either relieving the inhibition of BIRC proteins on caspases, leading to an increase in caspase activity; or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism (PubMed : 15200957). Cleaves BIRC6 and relieves its inhibition on CASP3, CASP7 and CASP9, but it is also prone to inhibition by BIRC6 (PubMed : 36758104, PubMed : 36758105). Cleaves THAP5 and promotes its degradation during apoptosis (PubMed : 19502560).. Isoform 2. Seems to be proteolytically inactive.
Sequence similarities
Belongs to the peptidase S1C family.
Post-translational modifications
Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC.. Autoproteolytically activated.
Subcellular localisation
Mitochondrion intermembrane space
Target data
Product promise
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