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|Description:||Transcreener 2-5A OAS Assay. The Transcreener OAS Assay measures the 2-5A produced by OAS1 (2'-5'-oligoadenylate synthetase 1) OAS2, or OAS3. These measurements allow researchers to effectively determine the activity of the OAS enzyme. The assay provides a powerful tool to screen compound libraries for OAS modulators to help find new therapies for disease. How Does This OAS Assay Work? The Transcreener OAS Assay determines OAS enzyme activity by using a coupling enzyme that converts 2'-5'A produced by OAS1 to the products AMP and ATP. AMP can be measured using the trusted Transcreener AMP2 Assay components. The assay provides a universal method to assess activity of any AMP-producing enzyme. Transcreener OAS Assay technology uses a simple but highly effective method that consists of an antibody selective to AMP and a far-red fluorescent tracer. AMP produced in the reaction competes with the tracer changing the fluorescent properties and providing fluorescent readout. The OAS assay is available with FP readout. It is a simple mix-and-read format. Perform your enzyme reaction, add the detection reagent, and measure. The simplicity of the system yields robust results that also makes it extremely amiable to HTS. The Role of OAS1 As a Therapeutic Target. Double-stranded RNA enters the cell from viruses. As a first line of defense, viral double-stranded RNA activates OAS1. OAS1 then synthesizes 2-5A from ATP, which activates RNase L. This signaling cleaves both viral and host RNA leading to inhibition of protein synthesis. The replication of invading RNA viruses ends. Mutation or inadvertent stimulation of OAS1 can produce autoimmune conditions by activating the pathway inconsistently, even while not in the presence of viral invaders. Because of this, OAS1 is an interesting target in drug discovery. The Transcreener OAS Assay is an excellent tool for researchers examining the therapeutic effects of OAS1.|
|Restrictions:||Only available in Germany and selected European countries.|
|More information:||Go to webpage|
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