The AlphaLISA® Human Immunodeficiency Virus type-1 p24 protein (HIV p24) (high sensitivity) Detection Kit is designed for detection and quantitation of HIV p24 in serum, buffered solution or cell culture medium in a homogeneous (no-wash steps, no separation steps) assay.
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Immunodeficiency Virus (HIV) p24 is the 231 amino acid phosphorylated protein of the capsid forming the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. p24 is a cleavage product of the p55 Gag polyprotein by viral proteases. HIV p24 and its 55 kDa precursor play a crucial role in the assembly, maturation, and disassembly of HIV. p24 can often be detected two weeks after infection. Subsequently, p24 antibody is produced and complexes with soluble p24 antigen, rendering it undetectable without first dissociating the antibody-antigen complex. Free antigen reappears later in the course of the illness as p24 antibody levels decline. p24 is frequently used for HIV detection in blood, serum samples, and other bodily fluids in acute HIV seroconversion, in neonatal infection, and for monitoring of responses to antiviral drug therapy.
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|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||5,000 assay points|
|Resource Type||File Name||File Format|
|Data Sheet||Manual AlphaLISA HIV p24 (High Sensitivity) AL291||PDF 219 KB|
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