IonGate Extends SURFE2R Workstation Family for Transporter Research with Compact, Entry-Level System
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IonGate Biosciences GmbH has announced the introduction of SURFE2R™ Workstation 5. This semi-automated, bench-top system, features the company’s proprietary SURFE2R (Surface Electrogenic Event Reader) technology and is designed for basic research and assay development.
The cell-free, biosensor-based system enables direct and precise measurement of transporter activity free of molecular labels, providing in-depth analysis of transporter function. The Workstation 5 provides one sensor position for a single sensor and up to 84 sample positions for buffers.
“SURFE2R technology is already gaining broad acceptance within the academic and pharmaceutical sectors. This new addition to the Workstation family replaces our successful SURFE2R One system, the first commercially available device to utilize IonGate’s revolutionary SURFE2R technology,” states Lars Eric Utterman, CEO of IonGate Biosciences.
“Following a major hardware redesign, and by embedding user-friendly control software, we have successfully reduced the system footprint and price to create a versatile, stand-alone, entry-level system. Workstation 5 has been developed to make SURFE2R technology more accessible to the academic sector, where bench space and budgets are limited. Workstations 50, 500 and 5000 provide the pharmaceutical industry with a wide range of throughput levels to suit their specific needs,” he concludes.
Besides being an ideal tool for the analysis of transporters, the technology is also complementary to conventional electrophysiology. “Although patch-clamping is currently the standard technique for measuring ion channels, there are some key, ion-conducting proteins that it simply cannot be applied to,” explains Dr. Petr Obrdlik, Head of Assay Development at IonGate Biosciences.
“It is not possible, for example, to measure the effects of drugs on the native intracellular vesicles and organelles, such as mitochondria, as standard patch-clamping equipment cannot access such membranes. Furthermore, the high sensitivity of SURFE2R technology enables detection of the activity of weakly electrogenic transport proteins, with efficiency levels superior to the standard patch-clamp approach,” concludes Dr. Obrdlik.
The cell-free, biosensor-based system enables direct and precise measurement of transporter activity free of molecular labels, providing in-depth analysis of transporter function. The Workstation 5 provides one sensor position for a single sensor and up to 84 sample positions for buffers.
“SURFE2R technology is already gaining broad acceptance within the academic and pharmaceutical sectors. This new addition to the Workstation family replaces our successful SURFE2R One system, the first commercially available device to utilize IonGate’s revolutionary SURFE2R technology,” states Lars Eric Utterman, CEO of IonGate Biosciences.
“Following a major hardware redesign, and by embedding user-friendly control software, we have successfully reduced the system footprint and price to create a versatile, stand-alone, entry-level system. Workstation 5 has been developed to make SURFE2R technology more accessible to the academic sector, where bench space and budgets are limited. Workstations 50, 500 and 5000 provide the pharmaceutical industry with a wide range of throughput levels to suit their specific needs,” he concludes.
Besides being an ideal tool for the analysis of transporters, the technology is also complementary to conventional electrophysiology. “Although patch-clamping is currently the standard technique for measuring ion channels, there are some key, ion-conducting proteins that it simply cannot be applied to,” explains Dr. Petr Obrdlik, Head of Assay Development at IonGate Biosciences.
“It is not possible, for example, to measure the effects of drugs on the native intracellular vesicles and organelles, such as mitochondria, as standard patch-clamping equipment cannot access such membranes. Furthermore, the high sensitivity of SURFE2R technology enables detection of the activity of weakly electrogenic transport proteins, with efficiency levels superior to the standard patch-clamp approach,” concludes Dr. Obrdlik.
