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. 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.

Specificity:

PGR(Phospho-S400) polyclonal antibody detects endogenous levels of PGR protein only when phosphorylated at Ser400.

Alternative names:

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

Species reactivity:

Human,Rat,Mouse

Host:

Rabbit

Ig type:

1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.3.

Immunogen:

Synthetic phosphopeptide derived from human PGR around the phosphorylation site of Serine 400.

Purification & Purity:

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

Molecular weight:

~ 98 kDa

Applications:

WB

Usage:

WB: 1:500~1:1000

Storage:

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Precautions:

For research use only, not for use in diagnostic procedure.

More info:

Email: info@sobekbio.com

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