LifeSensors Launches DiUbiquitin Substrate
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LifeSensors, Inc., a biotechnology company, announces the launch of its physiologically-relevant diubiquitin substrates for measuring isopeptide bond cleavage after filing for patent applications.
This technology, for both basic research and drug discovery targeting the ubiquitin proteasome pathway, offers sensitive and robust fluorescent readouts of isopeptidase or de-ubiquitylase (DUB) activity.
Protein modification by the ubiquitin-proteasome system is a central mechanism involved in the regulation of critical cellular functions. De-ubiquitylases (DUBs) play a role in this regulation by cleaving the isopeptide linkage that joins the ubiquitin(s) to its target substrate. Currently, methods for measuring de-ubiquitylase activity utilize ubiquitin linked by a linear bond to small fluorophores .These substrates do not mimic true ubiquitin isopeptide bonds and have thus hindered drug discovery efforts.
In addition, these substrates do not distinguish the activity of certain DUBs for different types of polyubiquitin chain substrates. Measuring true isopeptide bond cleavage in a high throughput manner has been a vital missing component in DUB research.
LifeSensors announces the launch of a novel, internally quenched fluorescence (IQF) substrate for measuring DUB activity. These substrates utilize ubiquitin molecules linked by true isopeptide bonds, making them more physiologically relevant than previous substrates. These DiUbiquitins represent a new class of substrates for measuring cleavage of an isopeptide bond in a homogeneous and continuous assay platform. They can be used for standard biochemical (kinetic) assays and have also been validated for high throughput screening in 96- and 384 well plates.
This technology, for both basic research and drug discovery targeting the ubiquitin proteasome pathway, offers sensitive and robust fluorescent readouts of isopeptidase or de-ubiquitylase (DUB) activity.
Protein modification by the ubiquitin-proteasome system is a central mechanism involved in the regulation of critical cellular functions. De-ubiquitylases (DUBs) play a role in this regulation by cleaving the isopeptide linkage that joins the ubiquitin(s) to its target substrate. Currently, methods for measuring de-ubiquitylase activity utilize ubiquitin linked by a linear bond to small fluorophores .These substrates do not mimic true ubiquitin isopeptide bonds and have thus hindered drug discovery efforts.
In addition, these substrates do not distinguish the activity of certain DUBs for different types of polyubiquitin chain substrates. Measuring true isopeptide bond cleavage in a high throughput manner has been a vital missing component in DUB research.
LifeSensors announces the launch of a novel, internally quenched fluorescence (IQF) substrate for measuring DUB activity. These substrates utilize ubiquitin molecules linked by true isopeptide bonds, making them more physiologically relevant than previous substrates. These DiUbiquitins represent a new class of substrates for measuring cleavage of an isopeptide bond in a homogeneous and continuous assay platform. They can be used for standard biochemical (kinetic) assays and have also been validated for high throughput screening in 96- and 384 well plates.
