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In Situ Pan-Caspase Assay Kit, Sulforhodamine from CHEMICON

ProductsIn Situ Pan-Caspase Assay Kit, Sulforhodamine from CHEMICON
Item In Situ Pan-Caspase Assay Kit, Sulforhodamine
Price $489.00
Description Apoptosis is an evolutionarily conserved form of cell suicide, which follows a specialized cellular process. The central component of this process is a cascade of proteolytic enzymes called caspases. These enzymes participate in a series of reactions that are triggered in response to pro-apoptotic signals and result in the cleavage of protein substrates, causing the disassembly of the cell. Caspases have been identified in organisms ranging from C. elegans to humans. The mammalian caspases play distinct roles in apoptosis and inflammation. In apoptosis, caspases are responsible for proteolytic cleavages that lead to cell disassembly (effector caspases), and are involved in upstream regulatory events (initiator caspases). An active caspase consists of two large and two small subunits that form two heterodimers which associate in a tetramer. In common with other proteases, caspases are synthesized as precursors that undergo proteolytic maturation, either autocatalytically or in a cascade by enzymes with similar specificity. Caspase enzymes specifically recognize a 4 or 5 amino acid sequence on the target substrate which necessarily includes an aspartic acid residue. This residue is the target for cleavage, which occurs at the carbonyl end of the aspartic acid residue. Caspases can be detected via immunoprecipitation, immunoblotting techniques using caspase specific antibodies, or by employing fluorochrome substrates which become fluorescent upon cleavage by the caspase.
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... techniques are defined by the author of ... This valuable hardcover guide includes hundreds of ... references. More than 300 pages detail the ... preparation from selection and design of ...
... The active ingredient in Molecular Probes. ... appears to act as a free ... emission. Our original SlowFade formulation (S-2828) ... rate of fluorescein to almost zero ...
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