R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Androgen Receptor (AR-V7 Specific) (E3O8L) Rabbit mAb #19672
Filter:
- WB
- IP
- ChIP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 80 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:50 - 1:250 |
| Immunoprecipitation | 1:200 |
| Chromatin IP | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Androgen Receptor (AR-V7 Specific) (E3O8L) Rabbit mAb recognizes endogenous levels of total AR-V7 protein. This antibody does not cross-react with full-length AR protein, but immunoprecipitates a 120 kDa protein of unknown identity.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu639 of human androgen receptor (V7 isoform) protein.
Background
Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. Research studies have shown that AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).
The AR3 or AR-V7 isoform, which lacks the typical ligand binding domain, is created through the alternative splicing of cryptic exons (4-5). AR-V7 is frequently expressed in castration-resistant prostate cancer (CRPC) and while dependent on the activity of the full-length androgen receptor (AR-FL), AR-V7 can activate a completely distinct transcriptional program (6-8). While enzalutamide and abiraterone have been beneficial in treating CRPC through the ligand binding domain of AR-FL, resistance in patients has been shown to be associated with AR-V7 detection in circulating tumor cells (9-12). Studies probing into mechanisms of overcoming this resistance are currently being explored and may help in stratifying patient populations for more personalized therapies (13-15).
The AR3 or AR-V7 isoform, which lacks the typical ligand binding domain, is created through the alternative splicing of cryptic exons (4-5). AR-V7 is frequently expressed in castration-resistant prostate cancer (CRPC) and while dependent on the activity of the full-length androgen receptor (AR-FL), AR-V7 can activate a completely distinct transcriptional program (6-8). While enzalutamide and abiraterone have been beneficial in treating CRPC through the ligand binding domain of AR-FL, resistance in patients has been shown to be associated with AR-V7 detection in circulating tumor cells (9-12). Studies probing into mechanisms of overcoming this resistance are currently being explored and may help in stratifying patient populations for more personalized therapies (13-15).
- Li, J. and Al-Azzawi, F. (2009) Maturitas 63, 142-8.
- Avila, D.M. et al. (2001) J. Steroid. Biochem. Mol. Biol. 76, 135-142.
- Montgomery, J.S. et al. (2001) J. Pathol. 195, 138-146.
- Hu, R. et al. (2009) Cancer Res 69, 16-22.
- Guo, Z. et al. (2009) Cancer Res 69, 2305-13.
- Watson, P.A. et al. (2010) Proc Natl Acad Sci U S A 107, 16759-65.
- Sun, S. et al. (2010) J Clin Invest 120, 2715-30.
- Hu, R. et al. (2012) Cancer Res 72, 3457-62.
- Scher, H.I. et al. (2012) N Engl J Med 367, 1187-97.
- de Bono, J.S. et al. (2011) N Engl J Med 364, 1995-2005.
- Ryan, C.J. et al. (2013) N Engl J Med 368, 138-48.
- Antonarakis, E.S. et al. (2014) N Engl J Med 371, 1028-38.
- Liu, C. et al. (2014) Clin Cancer Res 20, 3198-3210.
- Sarwar, M. et al. (2016) Oncotarget 7, 63065-63081.
- Ku, S.Y. et al. (2017) Science 355, 78-83.
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