Anti-Progesterone Receptor Antibody (OAAI00141)

Dry Ice

PGR

The progesterone receptor (PR) is a member of the steroid receptor superfamily. PR expression indicates a responsive estrogen receptor (ER) pathway, and therefore, may predict likely response to endocrine therapy in Human breast cancer. In Humans, the progesterone receptor (PR) gene gives rise to multiple isoforms. The a€œBa€ (PR-B, 116kDa, 933aa) contains a proline-rich N-term (aa 1 - 566), a central DNA-binding domain (DBD) (aa 567 - 636), a nuclear localization motif (aa 637 - 644), and a hormone binding/dimerization domain (HBD) (aa 645 - 933). PR-A (94 kDa, 769aa) utilizes a different start site that shortens the N-terminus by 164 amino acids. The N-terminus in both is rich in serine that is phosphorylated in response to hormone binding. In the absence of hormone, a few PR-A and -B molecules are phosphorylated at Serine 190 (S190).
Hormone increases this number two-fold, providing evidence for hormone stimulation. The common Serine at 294 can only be phosphorylated on PR-B, due to a difference in N-terminal conformation. This may account for functional differences between the molecules. Alternate start sites also geneRate two shorter forms that lack the N-terminus: PR-C (60 kDa, 339 aa), PR-M (38 kDa, 314aa). PR-A, -B and -C are known to heterodimerize. Alternate splicing of PR-A geneRates at least four other isoforms. All contain aa 1 - 516 (with the N-terminus), and are either truncated or show a partial deletion of the HBD.

The Rabbit IgG is purified by Epitope Affinity Purification.