Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Phospho-Progesterone Receptor (Ser190) Antibody #3171

Applications Reactivity Sensitivity MW (kDa) Source
W IP H Endogenous 90, 118 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-Progesterone Receptor (Ser190) Antibody detects endogenous levels of both progesterone receptor B and A forms only when phosphorylated at serine 190 and serine 26, respectively. This antibody does not cross-react with other PR family members.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser190 of human progesterone receptor. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from T47D cells, untreated or stimulated with 100 nM promegestone (R5020) for 1 hour, using Phospho-Progesterone Receptor (Ser190) Antibody (upper) and control Progesterone Receptor Antibody #3172 (lower).

Background

Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

  1. Evans, R.M. (1988) Science 240, 889-895.
  2. Kastner, P. et al. (1990) EMBO J. 112, 1603-1614.
  3. Giangrande, P.H. et al. (2000) Mol. Cell. Biol. 20, 3102-3115.
  4. Wen, D.X. et al. (1994) Mol. Cell. Biol. 14, 8356-8364.
  5. Clemm, D.L. et al. (2000) Mol. Endocrinol. 14, 52-65.
  6. Zhang, Y. et al. (1997) Mol. Endocrinol. 11, 823-832.
  7. Takimoto, G.S. et al. (1996) J. Biol. Chem. 271, 13308-13316.

Application References

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!

Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

Products