CST's PathScan® Phospho-cdc2 (Thr161) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-cdc2 (Thr161) protein. A Phospho-cdc2 (Thr161) Rabbit polyclonal Ab #9114* has been coated onto the microwells. After incubation with cell lysates, phospho-cdc2 (Thr161) protein is captured by the coated antibody. Following extensive washing, cdc2 Mouse mAb #2658* is added to detect the captured phospho-cdc2 protein. Anti-mouse IgG, HRP-linked Antibody #7076* is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-cdc2 (Thr161) protein.
* Antibodies in kit are custom formulations specific to kit.
CST's PathScan® Phospho-cdc2 (Thr161) Sandwich ELISA Kit detects endogenous levels of phospho-cdc2 (Thr161). As shown in Figure 1, using the Phospho-cdc2 (Thr161) ELISA Kit #7184, a significant induction of phospho-cdc2 (Thr161) is detected in HeLa cells treated with Interleukin-4. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).
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