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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb 4370 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry
H M R Hm Mk Mi Dm Z B Dg Pg Sc 44, 42 Rabbit IgG
Phospho-Progesterone Receptor (Ser190) Antibody 3171 40 µl
Western Blotting Immunoprecipitation
H 90, 118 Rabbit 
Phospho-Progesterone Receptor (Ser345) Antibody 12783 40 µl
Western Blotting
H 90 (PR-A), 118 (PR-B) Rabbit 
Progesterone Receptor A/B (D8Q2J) XP® Rabbit mAb 8757 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Chromatin Immunoprecipitation
H 90 (PR-A), 118 (PR-B) Rabbit IgG
Progesterone Receptor B (C1A2) Rabbit mAb 3157 40 µl
Western Blotting Immunohistochemistry Immunofluorescence Flow Cytometry
H 118 Rabbit IgG
Phospho-Src Family (Tyr416) (D49G4) Rabbit mAb 6943 40 µl
Western Blotting Immunoprecipitation
H M R Mk 60 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product 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.


Specificity / Sensitivity

Unless otherwise indicated, each antibody will recognize endogenous total levels of target protein. Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb recognizes endogenous p44 and p42 MAP Kinase (Erk1/2) when dually phosphorylated at Thr202/Tyr204 of Erk1 (Thr185/Tyr187 of Erk2), and singly phosphorylated at Thr202. This antibody does not cross-react with the corresponding phosphorylated residues of either JNK/SAPK or p38 MAP kinases. Phospho-Progesterone Receptor (Ser190) Antibody detects endogenous levels of progesterone receptors B and A only when phosphorylated at Ser190 and Ser26, respectively. Phospho-Progesterone Receptor (Ser345) Antibody recognizes endogenous levels of progesterone receptors B and A only when phosphorylated at Ser345 and Ser181, respectively. Phospho-Src Family (Tyr416) (D49G4) Rabbit mAb may cross-react with other Src family proteins phosphorylated at equivalent sites or with overexpressed phosphorylated RTKs.


Source / Purification

Monoclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr202/Tyr204 of human p44 MAP kinase, or with synthetic peptides corresponding to residues surrounding Ser115 or Tyr541 of human progesterone receptor protein, or Tyr416 of human Src protein. Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Ser190 of human progesterone receptor protein or Ser345 of human progesterone receptor B protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.

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, 889-895.

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.

8.  Faivre, E.J. et al. (2008) Mol Endocrinol 22, 823-37.

9.  Blunt, R.J. et al. (1975) Pflugers Arch 355, 189-204.


Entrez-Gene Id 5595, 5594, 2534, 3055, 3932, 4067, 5241, 6714, 7525
Swiss-Prot Acc. P27361, P28482, P06241, P08631, P06239, P07948, P06401, P12931, P07947

Protein Specific References

Syme CA et al. (2005) J Biol Chem 280, 11281–8

Li Z et al. (2001) J Biol Chem 276, 42226–32

Nguyen TH et al. (2002) J Biol Chem 277, 24274–9

Alonso A et al. (2004) J Biol Chem 279, 4922–8

Chichili GR and Rodgers W (2007) J Biol Chem 282, 36682–91

Wagner MJ and Smiley JR (2009) J Virol 83, 12452–61

Motiwala T et al. (2010) J Cell Biochem 110, 846–56

Jin LL et al. (2010) J Proteome Res 9, 2752–61

Shen T et al. (2001) Mol Cell Biol 21, 6122–31

Narayanan R et al. (2005) Mol Cell Biol 25, 2885–98

Daniel AR et al. (2007) Mol Endocrinol 21, 2890–906

Daniel AR and Lange CA (2009) Proc Natl Acad Sci U S A 106, 14287–92

Hagan CR et al. (2011) Mol Cell Biol 31, 2439–52

Busia L et al. (2011) Mol Cell Endocrinol 333, 37–46

Hagan CR et al. (2013) Nucleic Acids Res 41, 8926–42

Lange, C.A. et al. (2000) Proc Natl Acad Sci U S A 97, 1032-7.

Shen T et al. (2001) Mol Cell Biol 21, 6122–31

Narayanan R et al. (2005) Mol Cell Biol 25, 2885–98

Daniel AR et al. (2007) Mol Endocrinol 21, 2890–906

Daniel AR and Lange CA (2009) Proc Natl Acad Sci U S A 106, 14287–92

Hagan CR et al. (2011) Mol Cell Biol 31, 2439–52

Busia L et al. (2011) Mol Cell Endocrinol 333, 37–46

Hagan CR et al. (2013) Nucleic Acids Res 41, 8926–42

Lange, C.A. et al. (2000) Proc Natl Acad Sci U S A 97, 1032-7.

Shen T et al. (2001) Mol Cell Biol 21, 6122–31

Narayanan R et al. (2005) Mol Cell Biol 25, 2885–98

Daniel AR et al. (2007) Mol Endocrinol 21, 2890–906

Daniel AR and Lange CA (2009) Proc Natl Acad Sci U S A 106, 14287–92

Hagan CR et al. (2011) Mol Cell Biol 31, 2439–52

Busia L et al. (2011) Mol Cell Endocrinol 333, 37–46

Hagan CR et al. (2013) Nucleic Acids Res 41, 8926–42

Lange, C.A. et al. (2000) Proc Natl Acad Sci U S A 97, 1032-7.

Wang YH et al. (2001) Am J Physiol Cell Physiol 281, C1667–75

Schmitt JM and Stork PJ (2002) Mol Cell 9, 85–94

Abrahamsen H et al. (2003) J Biol Chem 278, 17170–7

Kim M et al. (2004) Oncogene 23, 1645–55

Zhou S et al. (2004) J Biol Chem 279, 54463–9

Ren Y et al. (2004) J Biol Chem 279, 8497–505

Kim HP et al. (2004) Biochem J 379, 141–50

Feistritzer C et al. (2005) Exp Cell Res 305, 214–20

Daoud G et al. (2006) J Physiol 571, 537–53

Eichhorn PJ et al. (2007) PLoS Genet 3, e218

Zhu S et al. (2007) Cancer Res 67, 10129–37

Zhou, J. et al. (2003) J Biol Chem 278, 6936-41.


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
XP® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.