What’s more, the perfect combination of UP-M-PCR and sequencing gel electrophoresis, as well as the optimization of the electrophoresis conditions, is another important innovative point in this study. With the dramatic expansion of global area under cultivation of GM crops, there is an urgent need to step up the development of robust, efficient, and reliable methods for GM detection. The developed UP-M-PCR method with sequencing gel electrophoresis analysis used to simultaneously detect nine commonly used selectable marker and reporter genes and six endogenous genes.A transcripts from the immunoglobulin heavy chain locus. At the molecular level, our data indicate that HOIP functions downstream of TRAF2 in the CD40 signaling pathway and that HOIP has a key role in promoting the recruitment of the IKK complex to CD40. Consistent with this, CD40-induced activation of NF-kB is dependent on the presence of HOIP. In addition, our data show that HOIP facilitates the activation of JNK in response to CD40 engagement. Together, our findings provide support for the conclusion that HOIP is a key component of the CD40 signaling pathway. Given the importance of CD40 signaling in both cellular and humoral immune responses, our results indicate that HOIP has a critical role in the regulation of the immune system. The functional properties of HOIP have only been partially characterized. Initial studies showed that HOIP and the related protein HOIL-1 are components of a large protein complex capable of synthesizing linear polyubiquitin chains. Subsequent studies showed that a HOIP-containing complex can interact with IKKc and facilitate activation of NF-kB via the canonical pathway. These data, considered together with ours, suggest that a HOIP-containing complex mediates recruitment of IKKc to the CD40 signaling complex. In addition, CD40- associated HOIP could play a role in activating IKKc after its recruitment to the signaling complex. The higher molecular weight forms of IKKc we observed in CD40 immunoprecipitates would be consistent with the presence of post-transcriptional modifications including HhAntag691 phosphorylation and ubiquitination, which have been suggested to reduce or enhance IKKc activity, respectively. The mechanisms by which HOIP mediates recruitment of the IKK complex to CD40 and by which HOIP is recruited to CD40 remain unclear. A previous study indicates that HOIP may mediate direct contacts with the IKK complex, suggesting that it functions as an adaptor for the recruitment of the IKK complex to CD40. However, the ubiquitin ligase activity of HOIP suggests that it is more than a simple adapter molecule.