p53 has been reported to mediate the down regulation of BCL2 either directly or indirectly through the NRE. As shown in Fig. 3B, the repression of SB1 on reporter gene was lowered if the first or natural product libraries third AT have been mutated to GC. However, the mut 2 construct repressed the reporter gene action to 32%, that was more significant than the repression induced by the construct without mutation. These data suggested that the repressive effect of SB1 was mediated by the first and third AT sites cooperatively, while the 2nd AT site was a key for the binding of SATB1, which mediated the antagonizing effect of the protein. Our research identifies a binding site, SB1, located between P1 and P2 area of the BCL2 gene. It possesses an innate transcriptional regulatory function in Jurkat cells and this function may be associated with the transcription factor SATB1. The region of NRE, that is located between 287 and Ribonucleic acid (RNA) 85 bp relative to the translation start site of the BCL2 gene, is known not just to reduce the reporter gene activity in Jurkat cells, but additionally to inhibit expression from the P1 promoter in pre B cells. The activity of the P1 promoter was higher in the absence of the NRE. Our new identified SATB1 binding site, SB1, is merely found within the NRE and may negatively control reporter gene activity. Therefore, SB1 may possibly contribute to the inhibitory effect of the NRE on P1 activity of the BCL2 gene. Because P1 is just a dominant ally of the BCL2 gene in Jurkat cells, we speculate that SB1 is a negative regulatory element that can down regulate BCL2 expression in Jurkat cells. It is known that SATB1 can recruit different transcription factors or chromatin remodeling factors to form protein complexes and manage a wide variety of genes. The significance of SB1 regulatory purpose and SATB1 was thus assessed with reporter gene system and RNAi trials. Interestingly, knockdown of SATB1 further increased the inhibitory effect of SB1 on the reporter gene Icotinib activity. It appears that the bad aftereffect of SB1 on transcription activity is independent of SATB1, but can be antagonized by SATB1 binding to SB1. There is little information regarding the negative regulatory components binding to the NRE. However, Jurkat is just a wild type p53 inferior cell lineand the consequence of p53 may be overlooked in this cell line. One candidate that may subscribe to the negative regulatory purpose of SB1 within NRE is Oct1, as bioinformatic analysis predicts that the third AT sites and first are both the key collection of Oct1 binding sites. Oct1 was initially identified as a factor that both positively or negatively regulates gene expression in numerous areas. In human T cells, Oct1 has been proven to act as a in concert with YY1 to down control IL 5 and CD21 transcription.