Product Pathways - Nuclear Receptor Signaling
Progesterone Receptor A/B (C89F7) Rabbit mAb #3153
|W IHC-P||H||Endogenous||90 (PR-A) and 118 (PR-B)||Rabbit IgG|
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.
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 blot analysis of extracts from T47D cells using Progesterone Receptor A/B (C89F7) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Progesterone Receptor A/B (C89F1) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded T47D cells (positive, left) and MDA-MB-231 cells (negative, right) using Progesterone Receptor A/B (C89F1) Rabbit mAb.
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.
- Evans, R.M. (1988) Science 240, 889-895.
- Kastner, P. et al. (1990) EMBO J. 112, 1603-1614.
- Giangrande, P.H. et al. (2000) Mol. Cell. Biol. 20, 3102-3115.
- Wen, D.X. et al. (1994) Mol. Cell. Biol. 14, 8356-8364.
- Clemm, D.L. et al. (2000) Mol. Endocrinol. 14, 52-65.
- Zhang, Y. et al. (1997) Mol. Endocrinol. 11, 823-832.
- Takimoto, G.S. et al. (1996) J. Biol. Chem. 271, 13308-13316.
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For Research Use Only. Not For Use In Diagnostic Procedures.