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Products:Epigenetics and Nuclear Signaling >> Transcription >> Domain Families >> Zinc Finger
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Read our guarantee »Anti-Progesterone Receptor antibody [alpha PR-22]
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Mouse monoclonal [alpha PR-22] to Progesterone Receptor
Detects the A and B forms of progesterone receptor (PR) from chicken and some species of turtles. This antibody does not cross-react with estrogen receptor or glucocorticoid receptor.
IP, WBmore details
Reacts with
Mouse, Chicken
Predicted to work with
Reptiles
Progesterone receptor (PR) purified from chick oviduct cytosol
Lyophilised:
Reconstitute with PBS.
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
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IgG fraction
Monoclonal
alpha PR-22
IgG2b
Cancer >> Tumor biomarkers >> Receptors
Cancer >> Signal transduction >> Nuclear signaling >> Nuclear hormone receptors >> Progesterone
Epigenetics and Nuclear Signaling >> Nuclear Signaling Pathways >> Nuclear Receptors >> Progesterone
Neuroscience >> Endocrine system >> Gonadotrophic axis
Signal Transduction >> Signaling Pathway >> Nuclear Signaling >> Nuclear Hormone Receptors >> Progesterone
Epigenetics and Nuclear Signaling >> Transcription >> Domain Families >> Zinc Finger
Our Abpromise guarantee covers the use of ab2767 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
IP: Use at an assay dependent dilution.
WB: Use at an assay dependent dilution. Detects a band of approximately 78, 110 kDa (predicted molecular weight: 99 kDa).
By Western blot, this antibody detects a 78 kDa protein representing the A form and a 110 kDa protein representing the B form of PR.
The proportion of receptor bound by this product is significantly greater than ab2765 due to the binding of both the A and B form of PR.
Protein A can effectively be used with this product in immunoprecipitation experiments.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
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.
Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation.
Belongs to the nuclear hormone receptor family. NR3 subfamily.
Contains 1 nuclear receptor DNA-binding domain.
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
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 G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1.
Sumoylation 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.
Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294.
Nucleus. Cytoplasm. Nucleoplasmic shuttling is both homone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases and Nucleus. Cytoplasm. Mainly nuclear.
Target information above from: UniProt accessionP06401
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
This product has been referenced in:
See all 11 publications for this product
Publishing research using ab2767? Please let us know so that we can cite the reference in this datasheet
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