EM5451
Anti-Estrogen Receptor α (Tyr-537), Phosphospecific Antibody
PhosphoSolutions
DETAILS
- Form: Antigen Affinity Purified
- Gene: ESR1
- Host: Mouse
- Rrid: AB_3068428
- Type: Primary Antibody
- Clone: M545
- Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
- Target: Estrogen Receptor α (Tyr-537)
- Isotype: IgG1
- 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: Mouse Monoclonal
- Immunogen: Clone M545 was generated from a phospho-ERα (Tyr-537) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding Tyr-537 in human ERα. This sequence is well conserved in rat and mouse ERα, and is also well conserved in ERβ (Tyr-488).
- 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 this reactivity is removed after alkaline phosphatase treatment.
- Applications: WB
- 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 Wb: 1:1000
- Immunogen Species: Human
- Species Reactivity: Chicken, Human, Mouse, Rat, and Xenopus
- 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
- Post Translational Modification Type: Phosphorylated
- Post Translational Modification Residue: Tyr-537