Anti-Progesterone Receptor antibody produced in chicken

PGR (progesterone receptor) is a member of nuclear receptor superfamily, the members of which act as transcription factors. It exists in two isoforms PRA and PRB. PRB contains an additional sequence of 164 amino acids at its N-terminal, which is absent in PRA. They have two activation function domains- AF-1 and AF-2. AF-1 is responsible for the activation of PGR-independent of ligand, whereas AF-2 mediates PGR-activation in a ligand-dependent manner. PRB also contains AF-3, present in the N-terminal. It has a variable N-terminal region, a DNA-binding domain, which is highly conserved in nature, and a ligand-binding domain at its C-terminal region. The DNA-binding domain and the ligand-binding domain are connected via a hinge domain. This gene is localized to human chromosome 11.q13.

Immunogen Sequence: GI # 31981492, sequence 61-350

Recombinant progesterone receptor

Anti-Progesterone Receptor antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.

The progesterone receptor (PR) protein is an inherent testicular protein and not a secretion of accessory reproductive organs. PR is expressed in human testis and in various reproductive tissues. It can serve as a marker to define the fertilizing potential of the spermatozoa. PR acts as an important marker for hormone dependence and disease prognosis. It is expressed in prostate stromal cells, where it regulates cell motility. Down-regulation of this protein in prostate stromal cancer cells, might lead to increased stromal derived factor-1 (SDF-1) and interlukin-6 (IL-6) levels, which in turn might promote tumor progression. In breast cancer, PGR and activator protein 1 (AP-1) nuclear interaction serves as a marker of favorable prognosis and overall patient survival, in cases treated with tamoxifen.

Solution in phosphate buffered saline containing 0.02% sodium azide.

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