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Caspase-3 shares many of the typical characteristics common to all currently-known caspases. For example, its active site contains a cysteine residue (Cys-163) and histidine residue (His-121) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid sequence.
“M30” is not a biological entity expressed in cells but a (patent protected) monoclonal antibody. Caspase-cleaved fragment of keratin 18 = ccK18 Keratin 18 = K18 (or CK18) M30® = the antibody that recognizes a neoepitope on ccK18 M65® ELISA = an ELISA composed of two antibodies (M5 and M6) for conventional epitopes of K18
Simple explanation of the mechanisms of apoptosis triggered by internal signals (bcl-2), along the caspase-9, caspase-3 and caspase-7 pathway; and by external signals (FAS and TNF), along the caspase 8 pathway. Accessed 25 March 2007. Apoptosis & Caspase 7, PMAP-animation; Caspases at the U.S. National Library of Medicine Medical Subject ...
ICAD has two caspase recognition sites at Asp117 and Asp224. CAD release from ICAD inhibition is achieved by cleavage of ICAD at these Asp residues by the caspase-3. [20] Caspase-3 is activated in the apoptotic cell. [9] Caspase-3 activation is a cell requirement during early stages of the skeletal myoblast differentiation.
During apoptosis, the apoptotic effector caspase, caspase-3, cleaves ICAD and thus causes CAD to become activated. [7] A nucleosome, consisting of DNA (grey) wrapped around a histone tetramer (coloured). In apoptotic DNA fragmentation, the DNA is cleaved in the internucleosomal linker region, which is the part of the DNA not wrapped around the ...
Active caspase-3 and -7 coimmunoprecipitated with survivin. The inactive proforms of caspase-3 and -7 did not bind survivin. [9] Survivin also does not bind to active caspase-8. [9] Caspase-3 and -7 are effector proteases whereas caspase-8 is an initiator caspase that sits more upstream in the apoptotic pathway. [9]
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