Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Progesterone Receptor B Antibody #3178

Applications Reactivity MW (kDa) Source
W H 118 Rabbit

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

Specificity / Sensitivity

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

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Thr73 of human progesterone receptor.

Western Blotting

Western Blotting

Western blot analysis of extracts from T47D and MCF-7 cells using Progesterone Receptor 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.

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