Estrogen Receptor α (Tyr-537), Phosphospecific Antibody
Référence bsm-70494M
Conditionnement : 100uL
Marque : Bioss
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Applications
Reactivity
| Overview | |
| Catalog # | bsm-70494m |
| Product Name | Estrogen Receptor _ (Tyr-537), Phosphospecific Antibody |
| Applications | WB |
| Specificity | 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 this reactivity is removed after alkaline phosphatase treatment. This sequence is well conserved in rat and mouse ER_, and is also well conserved in ER_ (Tyr-488). |
| Reactivity | Human, Mouse, Rat, Chicken, Xenopus |
| Specifications | |
| Conjugation | Unconjugated |
| Host | Mouse |
| Source | Clone M545 was generated from a phospho-ER_ (Tyr-537) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding Tyr-537 in human ER_. |
| Modification Site | Tyr-537 |
| Clonality | Monoclonal |
| Clone # | M545 |
| Isotype | IgG1 |
| Purification | Antigen Affinity purification |
| Storage Buffer | PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage Condition | 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 | |
| Swiss Prot | P03372 |
| Synonyms | ESR, ESR1, ESRA, Estradiol receptor, Eralpha, ER |
| Background | 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 | |