E1528
雌激素受体-α 人
≥80% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution
产品名称
雌激素受体-α 人, ≥80% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution
recombinant
expressed in baculovirus infected insect cells
assay
≥80% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
66.4 kDa
packaging
vial of 211 pmol
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
human ... ESR1(2099)
Biochem/physiol Actions
激素诱导型转录因子，能够对组织生长和分化相关的基因发挥正性或负性调节作用。
激素诱导型转录因子，能够对组织生长和分化相关的基因发挥正性或负性调节作用。用于信号传导、类固醇生物化学和内分泌干扰物研究。
Physical form
溶于 50 mM Tris-HCl (pH 8.0)、500 mM KCl、2 mM DTT、1 mM EDTA、1 mM 原钒酸盐 和 10% 甘油中。
存储类别
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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
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
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
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