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Read our guarantee »Anti-Progesterone Receptor (phospho S294) antibody
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Rabbit polyclonal to Progesterone Receptor (phospho S294)
The antibody is specific for human progesterone receptor phosphorylated at Ser294.
Dot Blot, WBmore details
Reacts with
Human
Synthetic phosphopeptide corresponding to amino acids residues surrounding the phosphoSer294 of human progesterone receptor
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: None
Constituents: 50% Glycerol, 150mM Sodium Chloride, 10mM HEPES, 100µg/ml BSA
Concentration information loading...
Protein G purified
The antibody was purified by ammonium sulphate followed by Protein G affinity purification methods.
Polyclonal
IgG
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
Western blot - Progesterone Receptor (phospho S294) antibody (ab13878)
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Our Abpromise guarantee covers the use of ab13878 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Dot: 1/1000 - 1/2000.
WB: 1/1000 - 1/2000. Detects a band of approximately 110 kDa (predicted molecular weight: 99 kDa).
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).
Western blot - Progesterone Receptor (phospho S294) antibody (ab13878)

Predicted band size : 99 kDa
Western blot analysis of progesterone receptor using ab13878.
ab13878 has not yet been referenced specifically in any publications.
Publishing research using ab13878? Please let us know so that we can cite the reference in this datasheet
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