|Application ||WB, IHC, IF|
|Calculated MW||33310 Da|
|Other Names||Caspase-6, CASP-6, Apoptotic protease Mch-2, Caspase-6 subunit p18, Caspase-6 subunit p11, CASP6, MCH2|
|Target/Specificity||A synthetic peptide corresponding to residues in C-terminus of human Caspase-6 was used as immunogen. The antibody should recognize both pro-form and p11 subunit.|
|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-6 Antibody (C-term) 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 poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death.|
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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-6 is a major apoptotic executioner (1,2). It exists as a pro-domain protein and is cleaved by caspase-3 into two active subunits, an 18 kDa and a 10 kDa subunit (3). Caspase-6 cleaves among many different intracellular proteins, nuclear lamins. Lamins play a significant role in maintaining the integrity of the cell membrane, and their cleavage results in subsequent cellular breakdown and death (4).
1. Fernandes-Alnemri, T. et al. Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. Cancer Res. 55: 2737
2. Srinivasula, S. M. et al. The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. J Biol. Chem. 271: 27099
3. Slee, E. A. et al. Ordering the Cytochrome c-initiated Caspase Cascade: Hierarchical Activation of Caspases-2, -3, -6, -7, -8, and -10 in a Caspase-9-dependent Manner. J. Cell Biol. 144: 281
4. Takahashi, A. et al. Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc Natl Acad Sci U S A 93: 8395
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