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Human serum albumin (HSA) is a 66 kDa protein produced by the liver. HSA constitutes two thirds of the protein mass of serum and plays a key role in the transport of small molecules in the blood such as fatty acids, vitamins, hormones, divalent cations, and drugs. Another important function of HSA is to maintain osmotic pressure and pH in the blood. HSA is an important biomarker in kidney disease. In albuminuria, albumin is not reabsorbed properly by kidney glomeruli and is excreted in the urine. Generally, in hypoalbuminemia, a lower level of albumin in serum can be explained by a kidney disease, poor liver function, or inflammation.
AlphaLISA technology allows the detection of molecules of interest in a no-wash, highly sensitive, quantitative assay. In an AlphaLISA assay, a biotinylated anti-analyte antibody binds to the Streptavidin-coated Donor beads while another anti-analyte antibody is conjugated to AlphaLISA Acceptor beads. In the presence of the analyte, the beads come into close proximity. The excitation of the Donor beads causes the release of singlet oxygen molecules that triggers a cascade of energy transfer in the Acceptor beads, resulting in a sharp peak of light emission at 615 nm.
|Assay Target Class||Protein|
|Experimental Type||In vitro|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||5,000 assay points|
For the detection of three biomarkers in complex sample matrices, the AlphaLISA and Electrochemiluminescent (ECL) assay technologies were shown to have similar: Assay windows (linear dynamic range), Lower and upper detection limit, Intra-and inter-assay precision (lower % CV) The advantages of using AlphaLISA over ECL are: Shorter total assay duration No wash steps No shaking Lower sample volume requirement for equivalent performance Less expensive instrument and plates required
The AlphaLISA® assay is a homogeneous immunoassay alternative to classical ELISA. AlphaLISA assays were originally utilized to detect analytesin cell cultures upernatants or serum/plasma samples.