Product Pathways - Abs in PBS
Phospho-PLK (Ser137) Antibody #5070
| Applications | Reactivity | Source |
|---|---|---|
| E-P | H | Rabbit |
Applications Key:
E-P=ELISA (Peptide)
Reactivity Key:
H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Phospho-PLK (Ser137) Antibody can be used in high throughput kinase assays and drug discovery applications. It detects peptides derived from PLK phosphorylated at Ser137.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) derived from the sequence of PLK. Antibodies are purified by protein A and peptide affinity chromatography.
Description
This antibody is formulated in PBS (no BSA/no glycerol) and quality controlled for use in ELISA and other drug discovery applications. This is a sample antibody and intended for use by drug discovery scientists.
Background
At least 4 distinct polo-like kinases exist in mammalian cells: PLK1, PLK2, PLK3 and PLK4/SAK (1). PLK1 apparently plays many roles during mitosis, particularly in regulating mitotic entry and exit. The mitosis promoting factor (MPF), cdc2/cyclin B1, is activated by dephosphorylation of cdc2 (Thr14/Tyr15) by cdc25C. PLK1 phosphorylates cdc25C at Ser198 and cyclin B1 at Ser133 causing translocation of these proteins from the cytoplasm to the nucleus (2-5). PLK1 phosphorylation of Myt1 at Ser426 and Thr495 has been proposed to inactivate Myt1, one of the kinases known to phosphorylate cdc2 at Thr14/Tyr15 (6). Polo-like kinases also phosphorylate the cohesin subunit SCC1, causing cohesin displacement from chromosome arms that allow for proper cohesin localization to centromeres (7). Mitotic exit requires activation of the anaphase promoting complex (APC) (8), a ubiquitin ligase responsible for removal of cohesin at centromeres, and degradation of securin, cyclin A, cyclin B1, Aurora A and cdc20 (9). PLK1 phosphorylation of the APC subunits Apc1, cdc16 and cdc27 has been demonstrated in vitro and has been proposed as a mechanism by which mitotic exit is regulated (10,11).
- Nigg, E.A. (1998) Curr. Opin. Cell Biol. 10, 776-783.
- Toyoshima-Morimoto, F. et al. (2002) EMBO Rep. 3, 341-348.
- Toyoshima-Morimoto, F. et al. (2001) Nature 410, 215-220.
- Peter, M. et al. (2002) EMBO Rep. 3, 551-556.
- Jackman, M. et al. (2003) Nat. Cell Biol. 5, 143-148.
- Nakajima, H. et al. (2003) J. Biol. Chem. 278, 25277-25280.
- Sumara, I. et al. (2002) Mol. Cell 9, 515-525.
- Hauf, S. et al. (2001) Science 293, 1320-1323.
- Peters, J.M. (1999) Exp. Cell Res. 248, 339-349.
- Kraft, C. et al. (2003) EMBO J. 22, 6598-6609.
- Kotani, S. et al. (1998) Mol. Cell 1, 371-380.
Application References
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Companion Products
- 1300 PLK (Ser137) Biotinylated Peptide
This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.