Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Progesterone Receptor A/B (C89F7) Rabbit mAb #3153

Applications Reactivity Sensitivity MW (kDa) Isotype
W IHC-P H Endogenous 90 (PR-A) and 118 (PR-B) Rabbit IgG

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 (C89F7) Rabbit mAb detects endogenous levels of total progesterone receptor A and B proteins. This antibody does not cross-react with other PR family members. Non-specific staining of smooth muscle may be observed in paraffin-embedded tissues.

Source / Purification

Monoclonal antibody is 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 extracts from T47D cells using Progesterone Receptor A/B (C89F7) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Progesterone Receptor A/B (C89F1) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded T47D cells (positive, left) and MDA-MB-231 cells (negative, right) using Progesterone Receptor A/B (C89F1) Rabbit mAb.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Progesterone Receptor A/B (C89F1) Rabbit mAb in the presence of control peptide (left) or antigen-specific peptide (right).

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

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Companion Products

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

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