Article No
4815
Article No | 4815 |
Country Availability | SE, FI, DK, NO, IS, EE, LV, LT, FO, GL, RU |
Components | Cell Lysis Buffer, 2X Reaction Buffer, DTT, Substrate DEVD-AMC, Inhibitor DEVD-FMK, AMC (7-amino-4-methyl-coumarin) |
Description | APOPCYTO Caspase-3 Fluorometric Assay Kit |
Supplier | MBL International Corp. |
Additional Information | Caspases are members of the cysteine aspartic acid-specific protease family, which may be activated by a variety of signals including death receptor ligation, DNA damage, serum starvation, stress, and many more. Active caspases recognize a wide number of different substrates, leading to the activation of several different apoptotic pathways. For example, CAD (caspase-activated deoxyribonuclease), a protein involved in chromatin fragmentation into nucleosome units, is indirectly activated by caspase-3, while ICAD (inhibitor of caspase-activated deoxyribonuclease) is inactivated by caspase-3. The cleavage of several structural proteins by caspases leads to the unique apoptosis cell morphology of chromatin condensation, nucleus fragmentation and cytoplasmic integrity. Detection of caspase activity is recognized as a standard method to measure apoptosis activity. The most common method to measure caspase activity is via the fluorometric or colorimetric detection of the cleavage of caspase-specific substrates. |
Notes | Caspases are members of the cysteine aspartic acid-specific protease family, which may be activated by a variety of signals including death receptor ligation, DNA damage, serum starvation, stress, and many more. Active caspases recognize a wide number of different substrates, leading to the activation of several different apoptotic pathways. For example, CAD (caspase-activated deoxyribonuclease), a protein involved in chromatin fragmentation into nucleosome units, is indirectly activated by caspase-3, while ICAD (inhibitor of caspase-activated deoxyribonuclease) is inactivated by caspase-3. The cleavage of several structural proteins by caspases leads to the unique apoptosis cell morphology of chromatin condensation, nucleus fragmentation and cytoplasmic integrity. Detection of caspase activity is recognized as a standard method to measure apoptosis activity. The most common method to measure caspase activity is via the fluorometric or colorimetric detection of the cleavage of caspase-specific substrates. |
Product Type | Assay & Detection |
References | 1). Okada M, et al., Blood, 103, 2299 (2004) 2). Shibata MA, et al., Carcinogenesis, 25, 1887 (2004) 3). Takeda K, et al., J Biol Chem, 282, 7522 (2007) 4). Tanaka H, et al., J Am Soc Nephrol, 15, 3083 (2004) 5). Tokudome T, et al, Endocrinology, 145, 2458 (2004) |
Research Area | Cell Death |
Shipping Information | dry ice |
Size | 100 Assays |
Stability | see label |
Storage | -20°C. Please refer to datasheet for additional information |
Technical Specifications | Caspases are members of the cysteine aspartic acid-specific protease family, which may be activated by a variety of signals including death receptor ligation, DNA damage, serum starvation, stress, and many more. Active caspases recognize a wide number of different substrates, leading to the activation of several different apoptotic pathways. For example, CAD (caspase-activated deoxyribonuclease), a protein involved in chromatin fragmentation into nucleosome units, is indirectly activated by caspase-3, while ICAD (inhibitor of caspase-activated deoxyribonuclease) is inactivated by caspase-3. The cleavage of several structural proteins by caspases leads to the unique apoptosis cell morphology of chromatin condensation, nucleus fragmentation and cytoplasmic integrity. Detection of caspase activity is recognized as a standard method to measure apoptosis activity. The most common method to measure caspase activity is via the fluorometric or colorimetric detection of the cleavage of caspase-specific substrates. |
Product Page Updated | 2021-01-11T15:22:00.814Z |