| Product Includes | Product # | Quantity | Mol. Wt | Isotype/Source |
|---|---|---|---|---|
| Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb | 4370 | 40 µl | 44, 42 kDa | Rabbit IgG |
| Phospho-Progesterone Receptor (Ser190) Antibody | 3171 | 40 µl | 90, 118 kDa | Rabbit |
| Phospho-Progesterone Receptor (Ser345) Antibody | 12783 | 40 µl | 90 (PR-A), 118 (PR-B) kDa | Rabbit |
| Progesterone Receptor A/B (D8Q2J) XP® Rabbit mAb | 8757 | 40 µl | 90 (PR-A), 118 (PR-B) kDa | Rabbit IgG |
| Progesterone Receptor B (C1A2) Rabbit mAb | 3157 | 40 µl | 118 kDa | Rabbit |
| Phospho-Src Family (Tyr416) (D49G4) Rabbit mAb | 6943 | 40 µl | 60 kDa | Rabbit IgG |
| Anti-rabbit IgG, HRP-linked Antibody | 7074 | 100 µl | Goat |
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Description
Progesterone Receptor Signaling Antibody Sampler Kit provides an economical means of detecting total and active levels of progesterone receptor (PR) as well as the active forms of PR downstream targets. The kit contains enough primary antibody to perform four western blots per primary antibody.
Storage
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. Research studies have demonstrated ligand-dependent phosphorylation of PR-B at Ser345 is catalyzed by MAPK and plays an important role in mediating the proliferation of breast cancer cells. Investigators have shown that Ser345-phosphorylated PR-B associates with Sp1 to regulate EGFR and p21 transcription (8). PR signaling has been shown to crosstalk with other kinase signaling cascades. Upon stimulation and the subsequent interaction with estrogen receptor α and c-Src, PR-B has been shown to promote the activation of the Src/p21ras/Erk pathway (9).
- Evans, R.M. (1988) Science 240, 889-95.
- Kastner, P. et al. (1990) EMBO J 9, 1603-14.
- Giangrande, P.H. et al. (2000) Mol Cell Biol 20, 3102-15.
- Wen, D.X. et al. (1994) Mol Cell Biol 14, 8356-64.
- Clemm, D.L. et al. (2000) Mol Endocrinol 14, 52-65.
- Zhang, Y. et al. (1997) Mol Endocrinol 11, 823-32.
- Takimoto, G.S. et al. (1996) J Biol Chem 271, 13308-16.
- Faivre, E.J. et al. (2008) Mol Endocrinol 22, 823-37.
- Blunt, R.J. et al. (1975) Pflugers Arch 355, 189-204.
Background References
Trademarks and Patents
Limited Uses
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