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GR39

Anti-Estrogen Receptor β (Ab-2) Mouse mAb (9.88)

Synonym(s):

Anti-ER β

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antibody form

ascites fluid

Quality Level

clone

9.88, monoclonal

form

liquid

contains

≤0.1% sodium azide as preservative

species reactivity

human, rat, mouse

isotype

IgM

General description

Anti-Estrogen Receptor β (Ab-2), mouse monoclonal, clone 9.88, recognizes the ~53 kDa estrogen receptor β. Does not cross-react with the α receptor It is validated for use in WB and IP.
Mouse monoclonal antibody generated by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with NS-1 mouse myeloma cells. Recognizes the ~53 kDa estrogen receptor β protein.
Recognizes the ~53 kDa estrogen receptor β protein. Does not cross-react with estrogen receptor α.
Steroids regulate important neuronal functions including the organization of neural circuits during development and the regulation of synapse organization in the adult. Steroid hormones may promote cell survival and differentiation of both neurons and glial cells, regulate synaptogenesis, prevent synapse elimination, cause axonal and dendritic growth, and play a role during regeneration of the nervous system. Steroid hormone receptors are members of a large family of nuclear ligand-activated transcription factors that includes the androgen, estrogen, glucocorticoid, and progesterone receptors. In the absence of hormone, steroid receptors are associated in complexes with heat shock proteins and immunophilins. Steroid binding results in the dissociation of the heat-shock protein, receptor dimerization, and binding to specific hormone response elements (HRE) to produce a transcriptionally active complex that leads to the activation or repression of target genes. Steroid receptors are regulated by phosphorylation, however, modulation of kinase activity can also cause receptor activation in the absence of hormone. Recent evidence suggests that steroid receptor expression can be regulated by neurotrophins, and that steroids can regulate the expression of trophic factors and their receptors. In addition to the classical estrogen receptor α, a second estrogen receptor, designated estrogen receptor &beta, has been identified. Although initially identified from the rat prostate, estrogen receptor β is expressed in a variety of tissues including the brain. In vitro studies demonstrate that estrogen receptor α and estrogen receptor β form both homodimers and heterodimers. Additionally, in situ hybridization and immunohistochemical studies indicate that estrogen receptor α and β are coexpressed in certain neuronal populations, but also exhibit distinct non-overlapping expression in the nervous system.

Immunogen

recombinant, human estrogen receptor β

Application

Immunoblotting (1:1000)
Immunoprecipitation (1 μl)
Paraffin Sections (not recommended)

Physical form

Undiluted ascites.

Preparation Note

Following initial thaw, aliquot and freeze (-20°C).

Analysis Note

Positive Control
Recombinant human estrogen receptor β protein, PC12 cells, or mouse brain

Other Notes

Does not cross-react with estrogen receptor α protein. Antibody should be titrated for optimal results in individual systems.




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N L Weigel
The Biochemical journal, 319 ( Pt 3), 657-667 (1996-11-01)
The steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors encompasses not only the receptors for steroids, thyroid hormone, retinoids and vitamin D, but also a large number of proteins whose functions and/or ligands are unknown and which are thus termed
K Pettersson et al.
Molecular endocrinology (Baltimore, Md.), 11(10), 1486-1496 (1997-09-01)
The recent discovery that an additional estrogen receptor subtype is present in various rat tissues has advanced our understanding of the mechanisms underlying estrogen signaling. Here we report on the cloning of the cDNA encoding the mouse homolog of estrogen
W B Pratt et al.
Endocrine reviews, 18(3), 306-360 (1997-06-01)
We have provided a historical perspective on a body of steroid receptor research dealing with the structure and physiological significance of the untransformed 9S receptor that has often confused both novice and expert investigators. The frequent controversies and equivocations of