Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A mouse DNase that causes DNA fragmentation was identified recently and designated CAD (for caspase activated deoxyribonuclease) (Enari et al. 1998; Sakahira et al. 1998). The human homologue of mouse CAD was more recently identified by three groups independently and termed CPAN and DFF40 and human CAD, respectively (Halenbeck et al. 1998; Liu et al. 1998; Mukae et al. 1998). DFF45/ICAD is the inhibitory protein of DFF40/CAD (Enari et al. 1998; Sakahira et al. 1998; Liu et al. 1997) and forms complex with DFF40/CAD. Upon cleavage of DFF45/ICAD by activated caspase, DFF40/CAD is released and activated and eventually cuases the degradation of DNA in the nuclei. Activation of DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death.
Immunogen
A peptide corresponding to amino acids 147-164 of mouse CAD (Enari et al. 1998). The sequence differs from human DFF40 by two amino acids (Halenbeck et al. 1998; Liu et al. 1998).
Application
Detect DFF40 using this Anti-DFF40 Antibody validated for use in WB.
Western blot: 1:500-1:1,000
K562 or Jurkat whole cell lysate can be used as a positive control and a 40 kDa band should be detected.
Optimal working dilutions must be determined by end user.
Physical form
Format: Purified
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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In addition to terminating neurotransmission by hydrolyzing acetylcholine, synaptic acetylcholinesterase (AChES) has been found to have a pro-apoptotic role. However, the underlying mechanism has rarely been investigated. Here, we report a nuclear translocation-dependent role for AChES as an apoptotic deoxyribonuclease
Proceedings of the National Academy of Sciences of the United States of America, 112(27), 8344-8349 (2015-06-25)
Cellular demolition during apoptosis is completed by executioner caspases, that selectively cleave more than 1,500 proteins but whose individual roles are challenging to assess. Here, we used an optimized site-specific and inducible protease to examine the role of a classic
The Journal of biological chemistry, 289(27), 18752-18769 (2014-05-20)
Caspase-dependent apoptosis is a controlled type of cell death characterized by oligonucleosomal DNA breakdown and major nuclear morphological alterations. Other kinds of cell death do not share these highly distinctive traits because caspase-activated DNase (DFF40/CAD) remains inactive. Here, we report
MLL (myeloid/lymphoid or mixed-lineage leukemia) rearrangements are frequent in therapy-related and childhood acute leukemia, and are associated with poor prognosis. The majority of the rearrangements fall within a 7.3-kb MLL breakpoint cluster region (MLLbcr), particularly in a 0.4-kb hotspot at
The Journal of biological chemistry, 288(13), 9200-9215 (2013-02-23)
Apoptotic nuclear morphology and oligonucleosomal double-strand DNA fragments (also known as DNA ladder) are considered the hallmarks of apoptotic cell death. From a classic point of view, these two processes occur concomitantly. Once activated, DNA fragmentation factor, 40-kDa subunit (DFF40)/caspase-activated
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