Overview |
bs-70492R |
Estrogen Receptor α (C-terminus) Antibody |
WB, IP, ICC |
This antibody detects several forms of ERα 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 |
ERα (C-terminus) synthetic peptide (coupled to carrier protein) corresponds to amino acids in the C-terminus of human ERα. This sequence is well conserved in rat and mouse ERα, but is not found in ERβ |
Polyclonal |
IgG |
Antigen Affinity purification |
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
Target |
P03372 |
ESR, ESR1, ESRA, Estradiol receptor, Eralpha, ER |
Estrogen receptor α (ERα) 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 ERα 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 ERα 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 ERα and degradation. Thus, a variety of phosphorylation events control ERα activity. |
Application Dilution |
WB |
1:300-5000 |
IP |
1-2ug |
ICC |
1:100-500 |