M30 CytoDEATH (RUO)

Cellular death caspase substrate Keratin 18 as valid apoptosis biomarker

Apoptosis induced by either death-inducing receptors or other stimuli leads to activation of specific caspases. Subsequently, apoptotic cells are eliminated by an intrinsic suicide program, resulting in DNA fragmentation, nuclear condensation, cytoskeletal reorganization, plasma membrane blebbing and loss of cell adhesion.
Keratin 18 (K18) is a type I intermediate filament protein and the major component of single-layer and glandular epithelial cells. It is expressed in most types of carcinomas such as lung, liver, prostate, breast and colon, whereas K18 is absent in lymphoid and neuronal cells and tissues. During apoptosis after initiation of effector caspases 3, 6, 7 and 9, K18 is cleaved into proteolytic fragments liberating neo-epitopes (NE) at the cleavage sites (ccK18, K18F).

M30 CytoDEATH™ antibody for the specific detection of apoptosis

K18 is cleaved by capases, liberating a neo-epitope (M30) that is specifically recognized by the M30 CytoDEATH™ monoclonal antibody. Specific proteolytic cleavage of K18 is an event taking place before disruption of membrane asymmetry and DNA strand breaks occur. Numerous studies confirm that M30 CytoDEATH™ antibody detects only apoptotic but not viable or necrotic cells. Reactivity of M30 CytoDEATH™ antibody in immunohistochemistry is associated with the apoptosis index by TUNEL and shows superior reliability in conditions when DNA double-strand breaks occur independent of apoptosis.

The capacity of M30 CytoDEATH™ antibody in flow cytomery and immuno-histochemistry studies to distinguish between necrotic and apoptotic epithelial cells has been verified in several disease entities. Consequently, M30 CytoDEATH™ antibody represents a unique tool for easy and reliable determination of apoptosis from very early until well advanced stages in single cells and tissue sections of epithelial origin.