| Product Name | Anti-PGR Polyclonal Antibody |
|---|---|
| Description | 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 . 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. |
| Host | Rabbit |
| Isotype | IgG |
| Reactivity | Human |
| Applications | ELISA, IHC, WB |
| Form | Liquid, in PBS with 0.02% sodium azide, 50% glycerol, pH 7.3. |
| Storage | Store at -20C or -80C. Avoid repeated freeze/thaw cycles. |
| 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 . 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. |
| Supplier | Cusabio |
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