PLK1 phospho T210 Antibody

Affinity Purified Plk1 pT210 was used at a 1:200 dilution to detect Plk1 by immunohistochemistry in human breast carcinoma tumor tissue. Tissue was formalin-fixed and paraffin embedded.

Affinity Purified Plk1 pT210 was used at a 1:200 dilution to detect Plk1 by immunohistochemistry in human colon carcinoma tumor tissue. Tissue was formalin-fixed and paraffin embedded.

Western blot analysis is shown to detect endogenous and recombinant protein present in HeLa cell lysates transfected with various plk-1 mutation constructs. Blots were reacted with anti-Plk-1 pT210 (panel A) and pan reactive anti-Plk-1 (panel B). Transfected cells were treated with 1 uM nocodazole followed by cell collection, lysate preparation, SDS-PAGE and western blotting. Using a 1:1000 dilution, anti-Plk-1 pT210 detects a single band corresponding to endogenous plk-1, but does not detect recombinant forms of the protein presumably because of a lack of phosphorylation in these mutants.

Western blot analysis is shown using Biorbyt's Affinity Purified anti-Plk-1 pT210 antibody to detect endogenous protein present in a Mouse A20 whole cell lysate (arrowhead). Comparison to a molecular weight marker indicates a band of ~68 kDa corresponding to Plk-1 protein. It is suggested to use a nuclear extract from synchronized cells to greatly increase the abundance of this protein in preparations. The blot was incubated with a 1:500 dilution of the antibody at room temperature followed by detection using standard techniques.