Production and characterization of a rabbit monoclonal antibody against human CDC25C phosphatase.
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[1] C. Peng,et al. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. , 1997, Science.
[2] J. Rutka,et al. Current concepts in neuro-oncology: the cell cycle--a review. , 1997, Neurosurgery.
[3] G. Draetta,et al. Cdc25 protein phosphatases in cell proliferation. , 1997, Biochimica et biophysica acta.
[4] Xu Xu,et al. Roles of Active Site Residues and the NH-terminal Domain in the Catalysis and Substrate Binding of Human Cdc25 (*) , 1996, The Journal of Biological Chemistry.
[5] P. Beer-Romero,et al. Identification of an essential acidic residue in Cdc25 protein phosphatase and a general three‐dimensional model for a core region in protein phosphatases , 1996, Protein science : a publication of the Protein Society.
[6] K L Knight,et al. Rabbit monoclonal antibodies: generating a fusion partner to produce rabbit-rabbit hybridomas. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[7] E. Karsenti,et al. The role of cdc25 in checkpoints and feedback controls in the eukaryotic cell cycle , 1994, Journal of Cell Science.
[8] P. Wagner,et al. Putative dehydrogenase tms1 suppresses growth arrest induced by a p53 tumour mutant in fission yeast. , 1993, European journal of biochemistry.
[9] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.