|Application ||WB, IHC, IF|
|Calculated MW||34277 Da|
|Other Names||Caspase-7, CASP-7, Apoptotic protease Mch-3, CMH-1, ICE-like apoptotic protease 3, ICE-LAP3, Caspase-7 subunit p20, Caspase-7 subunit p11, CASP7, MCH3|
|Target/Specificity||A synthetic peptide corresponding to residues near N-terminus of human Caspase-7 was used as immunogen. The antibody should recognize both pro-form and p20 cleaved-form. The antibody does not cross-react with other Caspase family members.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Caspase-7 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly- 217' bond. Overexpression promotes programmed cell death.|
|Tissue Location||Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain|
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Provided below are standard protocols that you may find useful for product applications.
Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. Caspase-7 (CMH-1, Mch3, ICE-LAP3) is an effector caspase involved in the activation cascade for apoptosis execution (1,2,3). Pro-Caspase-7 is a 35-kDa protein localized to the cytoplasm and expressed in a variety of tissues and cell lines (1). Upon activation, Caspase-7 is translocated to the mitochondria, and proceeds to proteolytically cleave poly(ADP-ribose) polymerase (PARP) (2,3) and endoplasmic reticular-specific substrate, sterol regulatory element-binding protein 1 (4).
1. Duan, H., et al. J. Biol. Chem. 271: 1621-5 (1996)
2. Lippke, J.A., et al. J. Biol. Chem. 271: 1825-8 (1996)
3. Fernandes-Alnemri, T., et al. Cancer Res. 55: 6045-52 (1995)
4. Chandler, J.M., et al. J. Biol. Chem. 273: 10815-10818 (1998)
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