Cat#:PA-956F;Product Name:Rabbit Anti-Human Progesterone Receptor Antibody;Synonym:PGR; progesterone receptor; PR; NR3C3; Nuclear receptor subfamily 3 group C member 3;Background:Progesterone receptor (PR) is a member of the steroid receptor superfamily that includes receptors for several steroids, thyroid hormone, oxysterols, and fat-soluble vitamins. PR exits in two isoforms, PRA and PRB, that are expressed from a single gene as a result of transcription from two alternative promoters. Isoform PRB contains an N-terminal fragment of 164 amino acids that is not present in isoform PRA. Binding of progesterone to PR induces a conformational change resulting in dimerization of two ligand receptor complexes, increased receptor phosphorylation and binding of receptor dimers to specific hormone-responsive DNA elements. There is some evidence suggesting that the ratio between PRA and PRB is altered during tumourigenesis, such that PRA predominates. Approximately 60% of invasive breast carcinomas express PRA and/or PRB, and PR expression is regarded generally as a marker of intact ERα function.;Description:Rabbit Anti-Human Progesterone Receptor Polyclonal Antibody;Host Species:Rabbit;Species Reactivity:Human;Isotype:IgG1;Application:IHC;Storage:Store antibody products at 2-8°C. For long term storage, aliquot and freeze at -20°C. Avoid repeated freeze/thaw cycles;Usage:For Lab Research Use Only;
PGR; progesterone receptor; PR; NR3C3; Nuclear receptor subfamily 3 group C member 3
Gene Introduction:
Progesterone receptor (PR) is a member of the steroid receptor superfamily that includes receptors for several steroids, thyroid hormone, oxysterols, and fat-soluble vitamins. PR exits in two isoforms, PRA and PRB, that are expressed from a single gene as a result of transcription from two alternative promoters. Isoform PRB contains an N-terminal fragment of 164 amino acids that is not present in isoform PRA. Binding of progesterone to PR induces a conformational change resulting in dimerization of two ligand receptor complexes, increased receptor phosphorylation and binding of receptor dimers to specific hormone-responsive DNA elements. There is some evidence suggesting that the ratio between PRA and PRB is altered during tumourigenesis, such that PRA predominates. Approximately 60% of invasive breast carcinomas express PRA and/or PRB, and PR expression is regarded generally as a marker of intact ERα function.