Revision 1
Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

Support: 877-678-TECH (8324)

Web: [email protected] cellsignal.com

3 Trask LaneDanversMassachusetts01923USA
For Research Use Only. Not for Use in Diagnostic Procedures.
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 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

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

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the 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 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).

  1. Evans, R.M. (1988) Science 240, 889-95.
  2. Kastner, P. et al. (1990) EMBO J 9, 1603-14.
  3. Giangrande, P.H. et al. (2000) Mol Cell Biol 20, 3102-15.
  4. Wen, D.X. et al. (1994) Mol Cell Biol 14, 8356-64.
  5. Clemm, D.L. et al. (2000) Mol Endocrinol 14, 52-65.
  6. Zhang, Y. et al. (1997) Mol Endocrinol 11, 823-32.
  7. Takimoto, G.S. et al. (1996) J Biol Chem 271, 13308-16.
  8. Faivre, E.J. et al. (2008) Mol Endocrinol 22, 823-37.
  9. Blunt, R.J. et al. (1975) Pflugers Arch 355, 189-204.

Background References

    Trademarks and Patents

    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    XP is a registered trademark of Cell Signaling Technology, Inc.
    All other trademarks are the property of their respective owners. Visit cellsignal.com/trademarks for more information.

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