AIF (D39D2) XP® Rabbit mAb (BSA and Azide Free) #62147
- WB
- IHC
- IF
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 67 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
AIF (D39D2) XP® Rabbit mAb (BSA and Azide Free) detects endogenous levels of total AIF protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Bovine, Dog
Source / Purification
Monoclonal antibody was produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala520 of human AIF protein.
Background
Apoptosis-inducing factor (AIF, PDCD8) is a ubiquitously expressed flavoprotein that plays a critical role in caspase-independent apoptosis (reviewed in 1,2). AIF is normally localized to the mitochondrial intermembrane space and released in response to apoptotic stimuli (3). Treatment of isolated nuclei with recombinant AIF leads to early apoptotic events, such as chromatin condensation and large-scale DNA fragmentation (3). Studies of AIF knockout mice have shown that the apoptotic activity of AIF is cell type and stimuli-dependent. Also noted was that AIF was required for embryoid body cavitation, representing the first wave of programmed cell death during embryonic morphogenesis (4). Structural analysis of AIF revealed two important regions, the first having oxidoreductase activity and the second being a potential DNA binding domain (3,5). While AIF is redox-active and can behave as an NADH oxidase, this activity is not required for inducing apoptosis (6). Instead, recent studies suggest that AIF has dual functions, a pro-apoptotic activity in the nucleus via its DNA binding and an anti-apoptotic activity via the scavenging of free radicals through its oxidoreductase activity (2,7).
- Daugas, E. et al. (2000) FEBS Lett 476, 118-23.
- Lipton, S.A. and Bossy-Wetzel, E. (2002) Cell 111, 147-50.
- Susin, S.A. et al. (1999) Nature 397, 441-6.
- Joza, N. et al. (2001) Nature 410, 549-54.
- Ye, H. et al. (2002) Nat Struct Biol 9, 680-4.
- Miramar, M.D. et al. (2001) J Biol Chem 276, 16391-8.
- Klein, J.A. et al. (2002) Nature 419, 367-74.
- Kozako, T. et al. (2015) Sci Rep 5, 11345.
Limited Uses
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