DFFA Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
---|---|
Primary Accession | O00273 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | H=37 KDa |
Isotype | Rabbit IgG |
Antigen Source | HUMAN |
Gene ID | 1676 |
---|---|
Antigen Region | 304-331 aa |
Other Names | DNA fragmentation factor subunit alpha, DNA fragmentation factor 45 kDa subunit, DFF-45, Inhibitor of CAD, ICAD, DFFA, DFF1, DFF45 |
Dilution | WB~~1:2000 |
Target/Specificity | This DFFA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 304-331 amino acids from the C-terminal region of human DFFA. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | DFFA Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | DFFA |
---|---|
Synonyms | DFF1, DFF45 |
Function | Inhibitor of the caspase-activated DNase (DFF40). |
Cellular Location | Cytoplasm. |
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Provided below are standard protocols that you may find useful for product applications.
Background
DFFA 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.
References
Ninios,Y.P., et.al., Apoptosis 15 (2), 128-138 (2010)
Banas,T., et.al., Eur. J. Obstet. Gynecol. Reprod. Biol. 146 (1), 87-91 (2009)
Trynka,G., et.al., Gut 58 (8), 1078-1083 (2009)
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