antibody

Rabbit anti Progesterone Receptor antibody

MBS462117

0.1 mg

350 USD

polyclonal

rabbit

nonconjugated

human, mouse, rat, cow

western blot, ELISA, immunohistochemistry

Antibody

Rabbit anti Progesterone Receptor antibody

Progesterone Receptor

Rabbit anti-PR

progesterone receptor; Progesterone receptor; progesterone receptor; OTTHUMP00000236114; OTTHUMP00000236115; OTTHUMP00000236117; OTTHUMP00000236119; nuclear receptor subfamily 3 group C member 3; progesterone receptor; Nuclear receptor subfamily 3 group C member 3

PGR; PGR; PR; NR3C3; NR3C3

PRGR_HUMAN

Rabbit

Human, Mouse, Rat, Bovine, Hamster

This antibody recognizes ~116 kDa of human PR protein. The other species are not tested

The Rabbit IgG is purified by Epitope Affinity Purification.

This affinity purified antibody is supplied in sterile Phosphate-buffered saline (pH7.2) containing antibody stabilizer

Size: 100 ug/200 ul

The antibodies are stable for 12 months from date of receipt when stored at -20 degree C to -70 degree C. Avoid repeated freezing-thawing cycles.

ELISA, Western Blot, Immunohistochemistry

Western Blot: 0.1-1 ug/ml. ELISA: 0.01-0.1 ug/ml. Immunoprecipitation: 2-5 ug/ml. Immunohistochemistry: 1-2 ug/ml

Antigen Preparation: A synthetic peptide corresponding to C-terminus of human Progesterone receptor.

Positive Control: Breast Cancer Tissue or MCF-7 cell. Cellular Location: Nuclear

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 "B" (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.

Zheng ZY, Lin VC. Anti-estrogenic effect of unliganded progesterone receptor is estrogen-selective in breast cancer cells MCF-7. Cancer Lett. 2008 May 12 (in press)

189935

P06401

116 kDa

Cellular Roles Of Anthrax Toxin Pathway (138076); Gene Expression Pathway (105937); Generic Transcription Pathway (105938); Nuclear Receptor Transcription Pathway (105979); Nuclear Receptors Pathway (198848); Oocyte Meiosis Pathway (126909); Oocyte Meiosis Pathway (126872); Ovarian Infertility Genes Pathway (198801); Progesterone-mediated Oocyte Maturation Pathway (119304); Progesterone-mediated Oocyte Maturation Pathway (503)

This gene encodes a member of the steroid receptor superfamily. The encoded protein mediates the physiological effects of progesterone, which plays a central role in reproductive events associated with the establishment and maintenance of pregnancy. This gene uses two distinct promotors and translation start sites in the first exon to produce two isoforms, A and B. The two isoforms are identical except for the additional 165 amino acids found in the N-terminus of isoform B and mediate their own response genes and physiologic effects with little overlap. [provided by RefSeq]

Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation. Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation. Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24. Subunit structure: Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and repesses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2 MAPK. Interacts with PRMT2. Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.24. Subcellular location: Nucleus. Cytoplasm. Note: Nucleoplasmic shuttling is both homone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G1 and G2/M phases. Ref.16 Ref.17 Ref.22Isoform A: Nucleus. Cytoplasm. Note: Mainly nuclear. Ref.16 Ref.17 Ref.22. Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. Post-translational modification: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.21 Ref.22 Ref.23 Ref.24Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294. Ref.19 Ref.20 Ref.21Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294. Sequence similarities: Belongs to the nuclear hormone receptor family. NR3 subfamily.Contains 1 nuclear receptor DNA-binding domain.

0.1 mg

350 USD