Immunohistochemistry (IHC) : Human breast carcinoma stained with anti-PR antibody using peroxidase-conjugate and DAB chromogen. Note the nuclear staining of tumor cells.

rabbit anti-PR monoclonal antibody (ZR4) 6434

$160.00 – $528.00

Antibody summary

Rabbit monoclonal to PR
Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
Reacts with: Human
Isotype:IgG
Control: Breast carcinomas
Visualization: Nuclear
0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted

SKU: 6434parent Category: antibody Tags: anatomy, Breast Pathology, monoclonal, PR

Weight	1 lbs
Dimensions	9 × 5 × 2 in
host	mouse
isotype	IgG
clonality	monoclonal
concentration	concentrate, predilute
applications	IHC
reactivity	human
available size	0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted

rabbit anti-PR monoclonal antibody ZR4 6434

antibody
Database link: human P06401
Tested applications IHC
Recommended dilutions As directed
Immunogen Recombinant fragment (around aa 1-200) of human PGR (exact sequence is proprietary)
Size and concentration 7 mL prediluted or 0.1, 0.5, 1.0 mL and concentrated
Form liquid
Storage Instructions 2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Purity affinity purified
Clonality monoclonal
Isotype IgG
Compatible secondaries goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863 goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control Rabbit polyclonal - Isotype Control

target relevance
Protein names Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3)
Protein family Nuclear hormone receptor family, NR3 subfamily
Mass 98981Da
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. Depending on the isoform, progesterone receptor functions as a transcriptional activator or repressor. {ECO:0000269\|PubMed:10757795, ECO:0000269\|PubMed:1587864, ECO:0000269\|PubMed:37478846, ECO:0000269\|PubMed:9407067, ECO:0000305}.; [Isoform A]: Ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity including repression of its isoform B, MR and ER. Transrepressional activity may involve recruitment of corepressor NCOR2. {ECO:0000269\|PubMed:7969170, ECO:0000269\|PubMed:8180103, ECO:0000269\|PubMed:8264658, ECO:0000305, ECO:0000305\|PubMed:10757795}.; [Isoform B]: Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000269\|PubMed:7969170}.; [Isoform 4]: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.
Subellular location Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases.; [Isoform A]: Nucleus. Cytoplasm. Note=Mainly nuclear.; [Isoform 4]: Mitochondrion outer membrane {ECO:0000269\|PubMed:23518922}.
Tissues In reproductive tissues the expression of isoform A and isoform B varies as a consequence of developmental and hormonal status. Isoform A and isoform B are expressed in comparable levels in uterine glandular epithelium during the proliferative phase of the menstrual cycle. Expression of isoform B but not of isoform A persists in the glands during mid-secretory phase. In the stroma, isoform A is the predominant form throughout the cycle. Heterogeneous isoform expression between the glands of the endometrium basalis and functionalis is implying region-specific responses to hormonal stimuli. {ECO:0000269\|PubMed:11041221}.
Structure Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and represses 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. Isoform A interacts with NCOR2. Isoform B (but not isoform A) interacts with NCOA2 and NCOA1. Isoform B (but not isoform A) interacts with KLF9. Interacts with GTF2B (PubMed:1517211). {ECO:0000250\|UniProtKB:Q00175, ECO:0000269\|PubMed:10757795, ECO:0000269\|PubMed:12039952, ECO:0000269\|PubMed:12917342, ECO:0000269\|PubMed:1517211, ECO:0000269\|PubMed:16478993, ECO:0000269\|PubMed:17020914, ECO:0000269\|PubMed:17347654, ECO:0000269\|PubMed:18202149}.
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 G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1. {ECO:0000269\|PubMed:10628747, ECO:0000269\|PubMed:10655479, ECO:0000269\|PubMed:11110801, ECO:0000269\|PubMed:15572662, ECO:0000269\|PubMed:15798179, ECO:0000269\|PubMed:17020914, ECO:0000269\|PubMed:17173941, ECO:0000269\|PubMed:17347654, ECO:0000269\|PubMed:17717077, ECO:0000269\|PubMed:18202149, ECO:0000269\|PubMed:7476977, ECO:0000269\|PubMed:8702648, ECO:0000269\|PubMed:9171245}.; 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. {ECO:0000269\|PubMed:10628747, ECO:0000269\|PubMed:10655479, ECO:0000269\|PubMed:15798179, ECO:0000269\|PubMed:17020914, ECO:0000269\|PubMed:17173941, ECO:0000269\|PubMed:17347654, ECO:0000269\|PubMed:17717077, ECO:0000269\|PubMed:18202149, ECO:0000269\|PubMed:8702648}.; Ubiquitination is hormone-dependent and represses sumoylation on the same site (PubMed:10628747, PubMed:10655479, PubMed:15798179, PubMed:17173941, PubMed:17717077, PubMed:18202149, PubMed:8702648). Promoted by MAPK-mediated phosphorylation on Ser-294 (PubMed:10628747, PubMed:10655479, PubMed:15798179, PubMed:17173941, PubMed:17717077, PubMed:18202149, PubMed:8702648). Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound PGR when it is not associated with coactivators (NCOAs) (PubMed:37478846). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (PubMed:37478846). {ECO:0000269\|PubMed:10628747, ECO:0000269\|PubMed:10655479, ECO:0000269\|PubMed:15798179, ECO:0000269\|PubMed:17173941, ECO:0000269\|PubMed:17717077, ECO:0000269\|PubMed:18202149, ECO:0000269\|PubMed:37478846, ECO:0000269\|PubMed:8702648}.; Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation. {ECO:0000269\|PubMed:22031296}.
Domain Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-term
Target Relevance information above includes information from UniProt accession: P06401
The UniProt Consortium

Data

Human breast carcinoma stained with anti-PR antibody using peroxidase-conjugate and DAB chromogen. Note the nuclear staining of tumor cells.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.