Anti-Estrogen Receptor (phospho S102) antibody (ab111917)
- Product nameAnti-Estrogen Receptor (phospho S102) antibodySee all Estrogen Receptor primary antibodies ...
- DescriptionRabbit polyclonal to Estrogen Receptor (phospho S102)
- Specificityab111917 detects endogenous levels of Estrogen Receptor only when phosphorylated at serine 102.
- Tested applicationsIHC-P more details
- Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthetic phosphopeptide derived from Human Estrogen Receptor around the phosphorylation site of serine 102 (L-N-SP-V-S).
- Positive controlHuman Breast carcinoma tissue.
- Storage instructionsStore at -20°C. Stable for 12 months at -20°C
- Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 49% PBS, 50% Glycerol, 0.88% Sodium chloride
- Concentration information loading...
- PurityImmunogen affinity purified
- Purification notesab111917 was affinity-purified from Rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site
- Clonality Polyclonal
Our Abpromise guarantee covers the use of ab111917 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||IHC-P: 1/50 - 1/100. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.|
- FunctionNuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Can activate the transcriptional activity of TFF1.
- Sequence similaritiesBelongs to the nuclear hormone receptor family. NR3 subfamily.
Contains 1 nuclear receptor DNA-binding domain.
- DomainComposed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
modificationsPhosphorylated by cyclin A/CDK2. Phosphorylation probably enhances transcriptional activity.
Glycosylated; contains N-acetylglucosamine, probably O-linked.
Ubiquitinated. Deubiquitinated by OTUB1.
Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization.
Palmitoylated (isoform 3). Not biotinylated (isoform 3).
- Cellular localizationNucleus. Cytoplasm. Cell membrane. A minor fraction is associated with the inner membrane and Nucleus. Cytoplasm. Cell membrane. Associated with the inner membrane via palmitoylation.
- Atherosclerosis, susceptibility to, included antibodyDKFZp686N23123 antibodyER Alpha antibody
- ER antibodyER Beta antibodyER-alpha antibodyER[a] antibodyER[b] antibodyEra antibodyERalpha antibodyErb antibodyErb2 antibodyERbeta antibodyESR antibodyESR BETA antibodyESR1 antibodyESR1_HUMAN antibodyESR2 antibodyESRA antibodyESRB antibodyEstr antibodyEstra antibodyEstradiol Receptor alpha antibodyEstradiol receptor antibodyEstradiol Receptor beta antibodyESTRB antibodyEstrogen receptor 1 (alpha) antibodyEstrogen Receptor 1 antibodyEstrogen receptor 2 (ER beta) antibodyEstrogen Receptor 2 antibodyEstrogen receptor 2 ER beta antibodyEstrogen receptor alpha antibodyEstrogen receptor antibodyEstrogen receptor beta 4 antibodyEstrogen resistance, included antibodyHDL cholesterol, augmented response of, to hormone replacement, included antibodyMyocardial infarction, susceptibility to, included antibodyNR3A1 antibodyNR3A2 antibodyNuclear receptor subfamily 3 group A member 1 antibodyNuclear receptor subfamily 3 group A member 2 antibodyOTTHUMP00000017718 antibodyOTTHUMP00000017719 antibodyRNESTROR antibody
Anti-Estrogen Receptor (phospho S102) antibody images
ab111917 at 1/50 dilution staining Estrogen Receptor in paraffin-embedded Human Breast carcinoma tissue by Immunohistochemistry. The image on the right is treated with the synthesized phosphopeptide.
References for Anti-Estrogen Receptor (phospho S102) antibody (ab111917)
ab111917 has not yet been referenced specifically in any publications.