D3438
Anti-DFF45, N-Terminal antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
别名:
Anti-ICAD
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 45 kDa (non-apoptotic cells)
species reactivity
human
technique(s)
western blot: 0.5 μg/mL using human HeLa cell extract
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... DFFA(1676)
General description
DFF exists as an inactive cytoplasmic protein until activated by apoptotic signals. DFF40, the nuclease responsible for DNA fragmentation during apoptosis, exists as a heterodimeric complex with DFF45.
Immunogen
synthetic peptide corresponding to amino acids 2-21 of the N-terminal region of human DFF45/ICAD (DNA Fragmentation Factor 45/Inhibitor of Caspase-3 Activated DNase I).
Application
Anti-DFF45 antibody produced in rabbit is suitable for immunoblotting at a working concentration of 0.5μg/mL using a total HeLa cell lysate.
Biochem/physiol Actions
DFF45 functions as both a chaperone, mediating the correct folding of DFF40, and an inhibitor of DFF40. DFF45 is cleaved by caspase-3 at two sites in response to apoptotic signals. This releases DFF40, the active nuclease. DFF40 seems to oligomerize, forming a large, functional complex which breaks down DNA by introducing double strand breaks. Also, DFF40 appears to interact directly with histone H1 that may stimulate its activity.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
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W Wöhrl et al.
Biochemical and biophysical research communications, 254(3), 552-558 (1999-01-28)
During apoptosis, changes to the nucleus of the dying cell include DNA degradation and structural collapse. These changes are accomplished by caspase-mediated cleavage of DNA-fragmenting factor DFF45, an inhibitor of the effector molecule DFF40. DFF45 and, more efficiently, a mutant
D Tang et al.
The Journal of biological chemistry, 273(44), 28549-28552 (1998-10-24)
Apoptosis involves the proteolysis of specific cellular proteins by a group of cysteine proteases known as caspases. Many of these cellular targets are either functionally inactivated (e.g. poly(ADP-ribose) polymerase) or activated (e.g. other caspases, gelsolin) by such processing, thereby facilitating
B B Wolf et al.
The Journal of biological chemistry, 274(43), 30651-30656 (1999-10-16)
Caspase-3 initiates apoptotic DNA fragmentation by proteolytically inactivating DFF45 (DNA fragmentation factor-45)/ICAD (inhibitor of caspase-activated DNase), which releases active DFF40/CAD (caspase-activated DNase), the inhibitor's associated endonuclease. Here, we examined whether other apoptotic proteinases initiated DNA fragmentation via DFF45/ICAD inactivation. In
X Liu et al.
The Journal of biological chemistry, 274(20), 13836-13840 (1999-05-13)
DNA fragmentation factor (DFF) is a heterodimeric protein composed of 45-kDa (DFF45) and 40-kDa (DFF40) subunits, a protein that mediates regulated DNA fragmentation and chromatin condensation in response to apoptotic signals. DFF45 is a specific molecular chaperone and an inhibitor
H Sakahira et al.
Nature, 391(6662), 96-99 (1998-01-09)
Various molecules such as cytokines and anticancer drugs, as well as factor deprivation, rapidly induce apoptosis (programmed cell death), which is morphologically characterized by cell shrinkage and the blebbing of plasma membranes and by nuclear condensation. Caspases, particularly caspase 3
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