What is cleaved caspase?
The cleaved-Caspase-3 (Asp175) antibody (referred to as cleaved-Caspase-3 antibody) from Cell Signaling Technology (Danvas, MA, USA) is a polyclonal antibody obtained from rabbit that was raised against a peptide in the large subunit of the human effector caspase, Caspase-3, amino-terminal to Asp175.
How is caspase-7 activated?
Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. It is activated upon cell death stimuli and induces apoptosis.
What is cleaved caspase 8?
Cleaved Caspase-8 (Asp374) (18C8) Rabbit mAb detects human Caspase-8 when cleaved at Asp374. This antibody will detect cleavage products containing the pro-domain with the p18 subunit as well as the p18 subunit alone. A band of unknown origin is detected at 25 kDa in some cell lines.
What is cleaved caspase 9?
Caspase-9 (ICE-LAP6, Mch6) is an important member of the cysteine aspartic acid protease (caspase) family (1,2). Cleaved caspase-9 further processes other caspase members, including caspase-3 and caspase-7, to initiate a caspase cascade, which leads to apoptosis (7-10). Duan, H. et al. (1996) J.
How are executioner caspases activated?
Initiator caspases are activated by intrinsic and extrinsic apoptopic pathways. This leads to the activation of other caspases including executioner caspases that carry out apoptosis by cleaving cellular components.
What proteins are cleaved by caspases?
Caspases are activated during apoptosis and cleave specific proteins, resulting in the irreversible commitment to cell death. The signal transduction proteins MEKK1, p21-activated kinase 2, and focal adhesion kinase are caspase substrates that contribute to the cell death response when cleaved.
What does caspase-8 do in apoptosis?
Activated caspase-8 is known to propagate the apoptotic signal either by directly cleaving and activating downstream caspases or by cleaving the BH3 Bcl2-interacting protein, which leads to the release of cytochrome c from mitochondria, triggering activation of caspase-9 in a complex with dATP and Apaf-1.
How does caspase-9 work?
Active caspase-9 works as an initiating caspase by cleaving, thus activating downstream executioner caspases, initiating apoptosis. Once activated, caspase-9 goes on to cleave caspase-3, -6, and -7, initiating the caspase cascade as they cleave several other cellular targets.
What caspase3 7?
The Caspase-Glo® 3/7 Assay(a,b) is a homogeneous, luminescent assay that measures caspase-3 and -7 activities. The assay provides a luminogenic caspase-3/7 substrate, which contains the tetrapeptide sequence DEVD, in a reagent optimized for caspase activity, luciferase activity and cell lysis.
How is Procaspase 9 activated?
Caspase-9 is activated by binding to Apaf-1, a multidomain adapter protein containing an N-terminal caspase recruitment domain (CARD), followed by a nucleotide-binding and oligomerization domain [13–16].