| First Author | Metzner M | Year | 2010 |
| Journal | PLoS One | Volume | 5 |
| Issue | 1 | Pages | e8883 |
| PubMed ID | 20111710 | Mgi Jnum | J:157620 |
| Mgi Id | MGI:4431282 | Doi | 10.1371/journal.pone.0008883 |
| Citation | Metzner M, et al. (2010) Two forms of activation-induced cytidine deaminase differing in their ability to bind agarose. PLoS One 5(1):e8883 |
| abstractText | BACKGROUND: Activation-induced cytidine deaminase (AID) is a B-cell-specific DNA mutator that plays a key role in the formation of the secondary antibody repertoire in germinal center B cells. In the search for binding partners, protein coimmunoprecipitation assays are often performed, generally with agarose beads. METHODOLOGY/PRINCIPAL FINDINGS: We found that, regardless of whether cell lysates containing exogenous or endogenous AID were examined, one of two mouse AID forms bound to agarose alone. CONCLUSIONS/SIGNIFICANCE: These binding characteristics may be due to the known post-translational modifications of AID; they may also need to be considered in coimmunoprecipitation experiments to avoid false-positive results. |
