Clone: AER311
Background: The human estrogen receptor has a molecular weight of 67 kDa and consists of 6 functional domains (domains A-F). Functional mapping of the estrogen receptor has determined a transcriptional promoting activity in the A/B domain. The hormone-binding domain (E domain) is located towards the carboxy terminal, whereas the DNA-binding domain (C domain) is found in the central portion of the molecule. It has been speculated that the presence in breast cancer cells of truncated forms of the estrogen receptor lacking the hormone-binding domain might promote the uncontrolled growth of the tumor.
Purification Method: Saturated ammonium sulphate precipitation.
Concentration: See vial for concentration
Source: Hybridoma produced by the fusion of splenocytes from mice immunized with purified estrogen receptors from calf uterus and mouse myeloma cells.
References: 1. Abbondanza, E., et al. 'Characterization and epitope mapping of a new panel of monoclonal antibodies to estradiol receptor.' Steroids 1993, 58, 4-12.2. Santeusanio, G., et al. 'Immunohistochemical analysis of estrogen receptors in breast carcinomas using monoclonal antibodies that recognize different domains of the receptor molecule.' Appl. Immunohistochem Mol Morphol. 2000, 8, 275-284.3. Hori, M., et al. 'Determination of estrogen receptor in primary breast cancer using two different monoclonal antibodies, and correlation with its mRNA expression.' Pathol. Int. 1999, 49, 191-197.4. Schuler, G., et al. 'Occurrence of estrogen receptor alpha in bovine placentomes throughout mid and late gestation and at parturition.' Biol. Reprod. 2002, 66, 976-982.
UniProt: P03372
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.