Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Progesterone Receptor A/B Antibody #3176

Applications Reactivity Sensitivity MW (kDa) Source
W IHC-P H Endogenous 90 (PR-A), 118 (PR-B) Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
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

Progesterone Receptor A/B Antibody detects endogenous levels of total progesterone receptor A and B proteins. This antibody does not cross-react with other PR family members.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr541 of human progesterone receptor.

Western Blotting

Western Blotting

Western blot analysis of T47D cell lysate using Progesterone Receptor A/B Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Progesterone Receptor A/B Antibody in the presence of control peptide (left) or antigen specific peptide (right).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded T47D cells (PR+) (left) vs. MDA-MB-231 cells (PR-) (right) using Progesterone Receptor A/B Antibody.


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 of 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

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Companion Products

This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.

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