AlphaLISA no-wash immunoassay kit for detection of human serum albumin (HSA) in urine, buffered solution, or cell culture medium.
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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.
Disclaimer: For research use only. Not for use in diagnostic procedures.
|Assay Target Class||Protein|
|Experimental Type||In vitro|
|One Unit Contains||5000 assay points|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||5,000 assay points|
|Resource Type||File Name||File Format|
|Data Sheet||Manual AlphaLISA Human Albumin AL294||PDF 203 KB|
|Poster||A Comparison of AlphaLISABead-Based Luminescence and Electrochemiluminescence Immunoassay Technologies for Detection of Human EPO, Amyloid Beta 42 and VEGF in Complex Sample Matrices||PDF 179 KB|
|Poster||AlphaLISA Assays are Homogeneous Sensitive Immunoassays for Detection of Analytesin a Variety of Biological Matrices||PDF 273 KB|