Human Apolipoprotein E kit
ApoE quantification in cells, supernatants and plasma
The cleaved PARP (Asp214) kit enables the specific and quantitative detection of endogenous levels of the human, mouse, and monkey large fragment (89-kDa) of PARP-1. With its central position downstream from caspases 3 and 7, both activated by extrinsic and intrinsic apoptosis pathways, cleaved PARP-1 represents a pertinent marker of cells undergoing apoptosis. Deregulated apoptosis plays a role in various diseases involving insufficient cell death, such as cancer, autoimmunity, and persistent infections, whereas excessive apoptosis can contribute to neuro-degeneration and ischaemia.
Two pathways activate the effector pro-caspase 3 that cleaved PARP on Asp214, leading to apoptosis:
- an extrinsic pathway (activated by death ligands like TNF alpha, FasL and ApoL that bind to their death receptors), activating the initiator procaspase-8
- an intrinsic pathway, or mitochondrial pathway (activated by cellular damage like stress, radiation, toxins, hypoxia and growth factor withdrawal), also activating pro-apoptotic factors like BAD, then the initiator procaspase-9
In response to death ligands or cell damage and activation of extrinsic or intrinsic apoptosis pathways, the nuclear enzyme PARP-1 (116 kDa) involved in the repair of damaged DNA is cleaved between Asp214 and Gly215 by activated caspases 3 and 7. The cleavage deactivates the enzyme by separating its N-terminal DNA binding domain p25 (24kDa) from its C-terminal catalytic domain p85 (89kDa), leading to DNA fragmentation and cell apoptosis. Cleaved PARP-1 is considered as an essential marker of apoptosis.
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