Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. (provided by RefSeq)
Immunogen
DFFA (NP_004392.1, 231 a.a. ~ 331 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
DNA fragmentation factor subunit α (DFFA) is a component of DNA fragmentation factor (DFF). It is mainly associated with apoptosis and genomic stability. Caspase-3-mediated cleavage of DFFA releases DFF40 (DNA fragmentation factor 40) which degrades chromosomal DNA. During menstruation, the apoptosis of endometrium cells is associated with DFFA. Its expression decreases after menopause. Silencing of DFFA increases doxorubicin effects in breast cancer cells.
MicroRNA-145 (miR-145) is considered to play key roles in many cellular processes, such as proliferation, differentiation and apoptosis, by inhibiting target gene expression. DNA Fragmentation Factor-45 (DFF45) has been found to be the substrate of Caspase-3, and the cleavage of
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