Specific for the ~90k PR-A isoform and the ~120k PR-B isoform phosphorylated at Ser294. Immunolabeling is blocked by the phosphopeptide used as the antigen but not by the corresponding dephosphopeptide.
Cross-Reactivity
Human
Predicted Reactivity
non-human primates
Purification
Protein G purified culture supernatant
Immunogen
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser294 conjugated to KLH
PGR
Reactivity: Human
IHC, StM
Host: Mouse
Monoclonal
PGR-2694
unconjugated
Application Notes
Recommended Dilution: WB: 1:1000 IHC (frozen sections, unpublished observations): 1:1000 Quality Control: Western blots performed on each lot.
Restrictions
For Research Use only
Format
Liquid
Buffer
100 μL in 10 mM HEPES ( pH 7.5), 150 mM NaCl, 100 μg per ml BSA and 50 % glycerol.
Storage
-20 °C
Target
Progesterone Receptor (PGR)
Alternative Name
PGR
Background
There is accumulating evidence to suggest that progesterone plays an essential role in the regulation of growth and differentiation of mammary glands and thus may play a key role in breast cancer (Edwards, 2005). The biological response to progesterone is mediated by two distinct forms of the human progesterone receptor (PR-A and PR-B forms). In most cell contexts, the B form functions as a transcriptional activator, whereas the A form functions as a transcriptional inhibitor of steroid hormones (Attia et al., 2000, Lin et al., 2003). Recently it has been demonstrated that there is differential hormone dependent regulation of the phosphorylation of the A and B forms of the receptor (Clemm et al., 2000) . Treatment of T47D breast cancer cells with progestin agonist increases the phosphorylation of Ser190 and Ser294 with different kinetics. These phosphorylation events may differentially affect the transcriptional activity of the receptor. Anti-Phospho Ser294 Progesterone Receptor Western blot of whole cell T47D lysate prepared from cells that had been incubated in the presence of the synthetic progestin agonist R5020 (500 nM) showing specific immunolabeling of the ~90k PR-A isoform and the ~120 PR-B isoform of the progesterone receptor phosphorylated at Ser294. The immunolabeling is blocked by the phosphopeptide used as the antigen (not shown).