Anti-Estrogen Receptor α (C-terminus) Antibody

DETAILS

Form: Antigen Affinity Purified
Gene: ESR1
Host: Rabbit
Rrid: AB_3068437
Type: Primary Antibody
Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Target: Estrogen Receptor α (C-terminus)
Isotype: IgG
Storage: 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.
Shipping: Blue Ice
Synonyms: ESR, ESR1, ESRA, Estradiol receptor, Eralpha, ER
Clonality: Rabbit Polyclonal
Immunogen: 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
Expiration: After date of receipt, stable for at least 1 year at -20°C.
Specificity: 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.
Applications: WB, ICC, IP
Conjugate Exem: Unconjugated
Physical State: Liquid
Quality Control: Western blots performed on each lot.
Usage Statement: For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
Molecular Weight: 35-66
Dilution Range Ip: 1:50
Dilution Range Wb: 1:500
Immunogen Species: Human
Dilution Range Icc: 1:100
Species Reactivity: Human, Mouse, and Rat
Target Description: 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.
Uniprot Number Immunogen Species: P03372