Synthetic phosphopeptide derived from human PGR around the phosphorylation site of Serine 400.
Conjugation:
Unconjugated
Alternative Names:
Progesterone receptor, PR, Nuclear receptor subfamily 3 group C member 3, PGR, NR3C3
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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.3.
Application Dilute:
WB: 1:500~1:1000
Application Notes:
PGR(Phospho-S400) polyclonal antibody detects endogenous levels of PGR protein only when phosphorylated at Ser400.
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