The AlphaLISA® Human Caspase-3 Detection Kit is designed for detection and quantitation of active caspase-3 in buffered solution or cell lysates, in a homogeneous (no-wash steps, no separation steps) assay.
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One antibody is specific for the cleaved (active) form of caspase-3: rabbit monoclonal antibody, clone number 9H19L2. The second antibody is specific to the full length protein: mouse monoclonal antibody, clone number 4-1-18.
Human caspase-3, also known as apopain, is a cysteine protease of 29 kDa. It is widely expressed and is an integral component of the apoptosis cascade. Caspase-3 is synthesized as an inactive proenzyme that is processed in cells undergoing apoptosis by self proteolysis and/or cleavage by other upstream proteases. Its cleavage generates a p17 and a p12 subunit. The p17/p12 heterodimer associates with itself to form a heterotetramer. Once active, caspase-3 cleaves key cellular proteins such as poly (ADP-ribose) polymerase, sterol regulatory element binding proteins, and other caspase members. Activation of caspase-3 is commonly used as a biomarker for assessment of apoptosis.
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 Active Caspase-3 AL278||PDF 287 KB|
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