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. Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription. 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. Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2. Mutation of Ser190 results in decreased activity of PR, suggesting that the phosphorylation at Ser190 may be critical to its biological function.

Progesterone receptor; PR; Nuclear receptor subfamily 3 group C member 3; PGR; NR3C3

p06401

Human

WB,IHC

WB 1:2000-1:5000
IHC 1:50-1:200

~ 125 kDa

Rabbit

This antibody detects endogenous levels of PR protein.

Synthetic peptide, corresponding to Human PR.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.