For research use only. Not for use in diagnostic procedures.
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The AlphaLISA® human PCSK9 and human LDLR binding assay uses anti-6xHis AlphaLISA Acceptor beads to capture the His-tagged PCSK9 and Streptavidin-coated Donor beads to capture the biotinylated LDLR. When PCSK9 binds LDLR, excitation of the Donor beads provokes the release of singlet oxygen that triggers a cascade of energy transfer reactions in the Acceptor beads, resulting in a sharp peak of light emission at 615 nm.
Human proprotein convertase subtilisin/kexin type 9 (PCSK9), also known as FH3, HCHOLA3, NARC1 and PC9, is a crucial player in the regulation of plasma cholesterol homeostasis. PCSK9 binds to low density lipoprotein receptor (LDLR) and promotes PCSK9 lysosomal degradation in the liver, thereby reducing LDL clearance. Studies of PCSK9-LDLR binding have aided in the development of therapeutic anti-PCSK9 antibodies that effectively block this interaction at the cell surface. Therefore, blocking PCSK9 and LDLR binding has been considered a promising therapeutic target against cardiovascular disease.
|Assay Target||PCSK9, LDLR|
|Assay Target Class||Protein|
|Experimental Type||In vitro|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||5,000 Assay Points|
Mouse pharmacological models continue to play a large role in the study of human disease, and mouse tool reagents have shown high utility in immunology and cancer research for decades. It can often be quicker to learn about immunology and the regulation of immune responses using a syngeneic mouse model. However, working in mouse systems can often require the development of separate mouse reagents, if the therapeutic agent of interest does not cross-react with mouse. Find out how the AlphaLISA® human PD-1/PD-L1 and AlphaLISA mouse PD-1/PD-L1 binding assays provide a fast, powerful, homogeneous platform for obtain binding potencies from potential novel drug candidates.
This guide presents the simple conversion of an ELISA or other immunoassay to an AlphaLISA® immunoassay.