Anti-Phospho-Estrogen Receptor alpha (S118) Antibody [SC05-87]

HUABIO

Anti-Phospho-Estrogen Receptor alpha (S118) Antibody [SC05-87]

7

ImmunoFluorescence, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin

WB,IF-Cell,IF-Tissue,IHC-P

Research Use Only

Monoclonal

SC05-87

1 mg/ml

Unconjugated

ESR1

estrogen receptor 1

ER, ESR, ESRA, ESTRR, Era, NR3A1, estrogen receptor, E2 receptor alpha, ER-alpha, estradiol receptor, estrogen nuclear receptor alpha, estrogen receptor alpha E1-E2-1-2, estrogen receptor alpha E1-N2-E2-1-2, nuclear receptor subfamily 3 group A member 1, oestrogen receptor alpha

Rabbit

IgG

Estrogen receptor

Estrogen receptor alpha (ERa, ER, ESR, ESRA, Era, NR3A1, estrogen receptor 1) is a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding and activation of transcription. Alternative splicing results in several ERa mRNA transcripts, which differ primarily in their 5 untranslated regions. ERa undergoes phosphorylation in response to estradiol binding. Human ERa is predominately phosphorylated on Ser 118 and to a lesser extent on Ser 104 and Ser 106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation occurs on Ser 118 and Ser 167. These serine residues are all located within the activation function 1 region of the N-terminal domain of ERa. In contrast, activation of protein kinase A increases the phosphorylation of Ser 236, which is located in the DNA-binding domain. Src kinase-dependent Tyr 537 phosphorylation may enhance estrogen binding to ERa. Mutation of Tyr 537 of the human ERa produces receptors having a range of constitutive activity.

Human, Mouse

Human,Mouse

-20°C,2°C to 8°C

41116161