AIM2 (D5X7K) Rabbit mAb #12948
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Protocol
Specificity / Sensitivity
AIM2 (D5X7K) Rabbit mAb recognizes endogenous levels of total AIM2 protein. An unknown band is detected at 22 kDa in some cell lines.
Species Reactivity:
Human
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:
Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys93 of human AIM2 protein.
Background
Absent in melanoma 2 (AIM2) is an interferon-inducible protein containing an amino-terminal pyrin domain and carboxy-terminal HIN-200 domain that functions in innate immunity and tumor progression (1). Expression of AIM2 can inhibit cell growth and tumor formation (2,3). Furthermore, the AIM2 gene has a high frequency of mutations associated with microsatellite-unstable colorectal cancers (4). AIM2 has a critical role in the activation of caspase-1, the protease responsible for the processing of pro-inflammatory cytokines IL-1β and IL-18. Caspase-1 activation is regulated by multi-protein complexes referred to as “inflammasomes” (5,6). Distinct inflammasome complexes have been described containing NLRP1/NALP1, NLRP3/NALP3, IPAF, and AIM2. The HIN-200 domain of AIM2 is responsible for binding to cytoplasmic double-stranded DNA, resulting in caspase-1 activation. (7-9). This inflammasome complex also involves binding of the pyrin domain of AIM2 to the CARD-domain protein ASC/TMS1, which then interacts directly with caspase-1. As a result, AIM2 has been demonstrated to be an important sensor for a number of different pathogens (10-12).
- DeYoung, K.L. et al. (1997) Oncogene 15, 453-7.
- Chen, I.F. et al. (2006) Mol Cancer Ther 5, 1-7.
- Patsos, G. et al. (2010) Int J Cancer 126, 1838-49.
- Woerner, S.M. et al. (2007) Genes Chromosomes Cancer 46, 1080-9.
- Schroder, K. and Tschopp, J. (2010) Cell 140, 821-32.
- Khare, S. et al. (2010) Crit Rev Immunol 30, 463-87.
- Roberts, T.L. et al. (2009) Science 323, 1057-60.
- Hornung, V. et al. (2009) Nature 458, 514-8.
- Fernandes-Alnemri, T. et al. (2009) Nature 458, 509-13.
- Jones, J.W. et al. (2010) Proc Natl Acad Sci USA 107, 9771-6.
- Fernandes-Alnemri, T. et al. (2010) Nat Immunol 11, 385-93.
- Kim, S. et al. (2010) Eur J Immunol 40, 1545-51.
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