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DFFA Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O00273 |
|---|---|
| Clone Names | 90921102 |
| Gene ID | 1676 |
|---|---|
| Other Names | DNA fragmentation factor subunit alpha, DNA fragmentation factor 45 kDa subunit, DFF-45, Inhibitor of CAD, ICAD, DFFA, DFF1, DFF45 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP9286b was selected from the C-term region of human DFFA. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. 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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