MGSSHHHHHH SSGLVPRGSH MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD GGTAWISQES FDVDETDSGA GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE WELALRLQQT QSLHSLRSIS ASKASPPGDL QNPKRARQDP T.
DFFA is a part of the DNA Fragmentation Factor (DFF), which is a heterodimeric protein composed of two subunits: DFFB (40 kDa) and DFFA (45 kDa) . The primary role of DFFA is to act as a substrate for caspase-3, an enzyme that plays a pivotal role in the execution phase of apoptosis . Upon activation by caspase-3, DFFA is cleaved, leading to the dissociation of its fragments from DFFB, which then triggers DNA fragmentation and chromatin condensation .
Apoptosis is a vital process in mammalian development, responsible for removing toxic or unnecessary cells . During apoptosis, cells undergo shrinkage, nuclear fragmentation, and degradation of chromosomal DNA into nucleosomal units . DFFA, when cleaved by caspase-3, activates DFFB, which in turn induces DNA fragmentation, a hallmark of apoptosis .
The DFFA gene is located on chromosome 1 (1p36.22) in humans . It has been found to have two alternatively spliced transcript variants encoding distinct isoforms . The gene is associated with several pathways, including the FAS signaling cascades and the TNFR1 pathway, which are crucial for apoptosis and cell survival .
Recombinant DFFA refers to the DFFA protein produced through recombinant DNA technology. This involves inserting the DFFA gene into an expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant DFFA is used in research to study its role in apoptosis and to develop potential therapeutic interventions.