| Overview |
| bs-70492r |
| Estrogen Receptor _ (C-terminus) Antibody |
| WB, IP |
| This antibody detects several forms of ER_ ranging from 66 to 35 kDa* on SDS-PAGE immunoblots of MCF-7 cells treated with pervanadate, and MDA-MB-231 cells. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Rabbit |
| ER_ (C-terminus) synthetic peptide (coupled to carrier protein) corresponds to amino acids in the C-terminus of human ER_. This sequence is well conserved in rat and mouse ER_, but is not found in ER_ |
| Polyclonal |
| #REF! |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| P03372 |
| ESR, ESR1, ESRA, Estradiol receptor, Eralpha, ER |
| Estrogen receptor _ (ER_) is a member of the steroid receptor superfamily and its structure includes an N-terminal ligand-independent transactivation domain (AF-1), a highly conserved DNA binding domain, and a C-terminal ligand-dependent transactivation domain (AF-2). AF-1 and AF-2 activate transcription independently and synergistically, and act in a promoter- and cell-specific manner. Phosphorylation at multiple sites provides an important mechanism to regulate ER_ activity. Ser-104, Ser-106, Ser-118, and Ser-167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ER_ activity. In addition to these sites, phosphorylation of Tyr-537 has been implicated in maximal hormone binding, dimerization, and transcriptional activity. Tyr-537, located in the AF-2 domain, is phosphorylated by c-Src leading to nuclear export of ER_ and degradation. Thus, a variety of phosphorylation events control ER_ activity. |
| Application Dilution |
| WB |
1:300-5000 |
| IP |
1-2ug |
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