Product Description
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Mitochondrial Hydroxyl Radical Detection Assay Kit (ab219931) is a sensitive fluorometric one-step assay to detect intracellular hydroxyl radical (OH·) in live cells.
Key facts
Detection method:Fluorescent,
Sample types:Suspension cells, Adherent cells,
Assay Platform:Microplate reader, Fluorescence microscope
Product details:
Mitochondrial Hydroxyl Radical Detection Assay Kit (ab219931) is a sensitive fluorometric one-step assay to detect intracellular hydroxyl radical (OH·) in live cells. The assay uses our OH580 probe: the probe is cell-permeable and selectively reacts with hydroxyl radical present in live cells to generate a red fluorescence signal that can be easily read at Ex/Em= 540/590 nm.
The assay can be performed within one hour and can be detected by fluorescence microscopy, microplate reader or high-content imaging. It can be easily adapted to use in 384-well microplate format.
The detection of intracellular hydroxyl radical is of central importance to understanding proper cellular redox regulation and the impact of its dysregulation on various pathologies. The hydroxyl radical (HO·) is one of the reactive oxygen species (ROS) highly reactive with other molecules to achieve stability. In general, hydroxyl radical is considered to be a harmful by-product of oxidative metabolism, which can cause molecular damage in living system. It shows an average lifetime of 10-9 s and can react with nearly every biomolecule such as nuclear DNA, mitochondrial DNA, proteins and membrane lipids.**Related products**Review the , or the full to learn about more assays for metabolites, metabolic enzymes, mitochondrial function, and oxidative stress, and also how to assay metabolic function in live cells using your plate reader.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Mitochondrial hydroxyl radicals often abbreviated as 'OH radicals' are highly reactive species that derive from the reduction of oxygen. These radicals are produced in the mitochondria the energy powerhouses of the cell and are part of reactive oxygen species (ROS). The precise mass of individual hydroxyl radicals is not typically measured but these small molecules play a critical role in cellular functions. Mitochondrial ROS detection is an area of intense study due to its implications in understanding cellular oxidative stress.
Biological function summary
The presence of hydroxyl radicals can lead to oxidative damage to vital macromolecules including DNA proteins and lipids. The mitochondria themselves are frequent sites of this damage. Hydroxyl radicals are not part of a specific molecular complex but interact with various other molecules within the cell initiating chain reactions that propagate oxidative damage. This kind of impairment is involved in the regulation of apoptosis and other cellular activities.
Pathways
These radicals are central to the oxidative stress pathway. The antioxidant system often counters their effects by reducing the potential damage to cellular structures. Proteins such as superoxide dismutase (SOD) and catalase are related to this pathway and play an important role in mitigating the detrimental effects of oxidative stress. These pathways ensure a delicate balance between ROS production and elimination important for maintaining cellular homeostasis.
Mitochondrial hydroxyl radicals have been linked to neurodegenerative diseases such as Alzheimer's and Parkinson's disease. The unregulated production of these radicals can lead to significant cellular damage contributing to the progression of these conditions. Proteins like amyloid-beta in Alzheimer's disease and alpha-synuclein in Parkinson's disease connect to hydroxyl radicals through oxidative stress mechanisms where excessive ROS contributes to protein aggregation and neuronal damage. Understanding the interaction of hydroxyl radicals with these proteins offers insights into potential therapeutic interventions.
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Collaboration
Tony Tang
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