Recent journals described the protein Nur77/TR3 which specifically binds to Bcl 2 however not Bcl xL. In a with Nur77/TR3, its protective function is lost by Bcl 2. Ergo, in the next group of studies, we examined the role of natural compound library all through Celecoxib induced apoptosis. However, an of Nur77/ TR3 in a reaction to Celecoxib was not seen. Neither could we detect an interaction between Nur77/TR3 and Bcl 2. Ergo, an engagement of Nur77/TR3 all through Celecoxibinduced apoptosis might be excluded. Since Bcl 2 and Bcl xL confirmed different affinities for Bim, we hypothesized that these two similar anti apoptotic proteins could also differ in their binding to Bak. Co immunoprecipitation reports with an antibody that preferably acknowledged the active conformation of Bak as well as with antibodies against Mcl 1, Bcl 2, and BclxL revealed that Bak interacted primarily with Mcl 1 and Bcl xL. Bcl 2:Bak complexes weren’t found in healthier Jurkat vector cells, nor in cells treated with Celecoxib. In Bcl xL overexpressing cells, more Bak denver precipitated with Bcl xL than in JurkatVector settings. In total,however, less Bak was precipitated with the activation specific antibodywhen compared to Jurkat vector or Bcl 2 overexpressing cells confirming previous observations that Bcl xL checks Celecoxib induced Bak activation and DCm dissipation. Remarkably, Bak was Chromoblastomycosis also coprecipitated with Bcl 2 in cells overexpressing Bcl 2. To calculate the affinity of the Bak conversation with the three different anti apoptotic meats, we changed the lysis conditions. The use of the much more resilient detergent Triton X 100 instead of the delicate CHAPS prevented complex formation between Bcl 2 and Bak. Incontrast, Bcl xL andMcl 1 co precipitatedwithBak even under harder lysis conditions. Similar results were obtained when Triton X 100 was reduced from 1% to 0. 2%. The final studies show that the relationship of Bak with Bcl xL orMcl 1 differs from that of Bak with Bcl 2. Taken together, the results show that Bcl 2 and Bcl xL do not interact in the same way with Bak in Jurkat cells. The various affinities to Bak may also explain why Bcl 2, as opposed to Bcl xL, didn’t protect from Celecoxib caused ALK inhibitor apoptosis. Members of the Bcl 2 protein family are essential regulators of survival and death during apoptosis induction through the intrinsic pathway. The COX 2 inhibitor Celecoxib along with several cytotoxic drugs, ionizing light, growth element withdrawal, and severe hypoxia trigger apoptosis through the mitochondrial pathway. Overexpression of anti apoptotic meats or inefficient service of the pro apoptotic ones improves cellular survival and accounts for resistance against diverse anti cancer treatments.