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E1528

Sigma-Aldrich

Estrogen Receptor-α human

≥80% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution

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MDL number:
MFCD00676964
NACRES:
NA.32

recombinant

expressed in baculovirus infected insect cells

Quality Level

200

Assay

≥80% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

66.4 kDa

packaging

vial of 211 pmol

UniProt accession no.

P03372

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... ESR1(2099)

Biochem/physiol Actions

Hormone-inducible transcription factor capable of acting positively or negatively in regulating genes involved in tissue growth and differentiation. For use in signal transduction, steroid biochemistry, and endocrine disruptor research.

Physical form

Solution in 50 mM Tris-HCl, pH 8.0, 500 mM KCl, 2 mM DTT, 1 mM EDTA, 1 mM orthovanadate, and 10% glycerol.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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G G Kuiper et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(12), 5925-5930 (1996-06-11)
We have cloned a novel member of the nuclear receptor superfamily. The cDNA of clone 29 was isolated from a rat prostate cDNA library and it encodes a protein of 485 amino acid residues with a calculated molecular weight of
G G Kuiper et al.
Endocrinology, 138(3), 863-870 (1997-03-01)
The rat estrogen receptor (ER) exists as two subtypes, ER alpha and ER beta, which differ in the C-terminal ligand binding domain and in the N-terminal transactivation domain. In this study we investigated the messenger RNA expression of both ER
S Mosselman et al.
FEBS letters, 392(1), 49-53 (1996-08-19)
A novel estrogen receptor (hereinafter referred to as ER beta) was cloned using degenerate PCR primers. A comparison of the amino acid sequence of ER beta with the "classical' ER (ER alpha) shows a high degree of conservation of the
K Paech et al.
Science (New York, N.Y.), 277(5331), 1508-1510 (1997-09-05)
The transactivation properties of the two estrogen receptors, ERalpha and ERbeta, were examined with different ligands in the context of an estrogen response element and an AP1 element. ERalpha and ERbeta were shown to signal in opposite ways when complexed

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