|Calculated MW||36085 Da|
|Other Names||Lymphokine-activated killer T-cell-originated protein kinase, Cancer/testis antigen 84, CT84, MAPKK-like protein kinase, Nori-3, PDZ-binding kinase, Spermatogenesis-related protein kinase, SPK, T-LAK cell-originated protein kinase, PBK, TOPK|
|Target/Specificity||A synthetic peptide corresponding to residues on the N-terminus of human PBK was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PBK (TOPK) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.|
|Tissue Location||Expressed in the testis and placenta. In the testis, restrictedly expressed in outer cell layer of seminiferous tubules.|
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Provided below are standard protocols that you may find useful for product applications.
A novel mitotic kinase, PDZ-binding kinase or PBK, which is upregulated in a variety of neoplasms including hematological malignancies, has been the focus of attention with a goal to understand its role in malignant conversion and to examine as a possible new therapeutic target in disparate types of cancer. Studies provide a plausible explanation for the role of PBK augmenting tumor cell growth following transient appearance in different types of progenitor cells in vivo (1). PBK is a newly identified member of a novel MEK3/6-related MAPKK that may be enrolled in the activation of lymphoid cells and support testicular functions (2). In vitro, PBK binds specifically to PDZ2 of hDlg through its C-terminal T/SXV motif. PBK and hDlg are phosphorylated at mitosis in HeLa cells, and the mitotic phosphorylation of PBK is required for its kinase activity. In vitro, cdc2/cyclin B phosphorylates PBK. This evidence shows how PBK could link hDlg or other PDZ-containing proteins to signal transduction pathways regulating the cell cycle or cellular proliferation (3).
1. Nandi AK, et al. Biochem Biophys Res Commun 358(1): 181-1 (2007)
2. Abe Y, et al. J Biol Chem 275(28):21525-31 (2000)
3. Gaudet S, et al. Proc Natl Acad Sci 97(10):5167-72 (2000)
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