Recombinant Human Estrogen Receptor alpha Protein

Cat. No.: rp175926

GRADE & PURITY Carrier Free, Azide Free, His Tag, ≥90%(SDS-PAGE)

Expression System

E. coli

Accession #

P03372

Protein Tag

N-His

Expression system

E. coli

Endotoxin Concentration

<1.0 EU/μg

Descripción general

Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.

Description：

ER alpha (Estrogen receptor alpha; also Estradiol receptor and NR3A1) is a 65-70 kDa member of the NR3 subfamily, nuclear hormone receptor family of proteins.  It is widely expressed, and serves as a strong activator of estrogen-responsive genes.  ER alpha is normally quiescent and bound to heat-shock proteins and immunophilins.  Following beta -estradiol binding, it becomes activated, either homodimerizes or heterodimerizes with ER beta, and binds to DNA with multiple coactivators.  Human ER alpha is 595 amino acids (aa) in length.  It contains a DNA binding region (aa 185-250), three NLSs (aa 256-260; 266-271; 299-303), a steroid-binding site (aa 351-543), a dimerization motif (aa 497-518), and an O-GlcNAc attachment around Thr575. Major phosphorylation sites exist at Tyr537, Ser167 and Ser118.  Multiple splice forms exist.  There is an 80 kDa isoform that shows a substitution (duplication) of aa 412-517 for Asp411, a second isoform with a deletion of aa 255-366, a third isoform with a deletion of aa 152-412, and a fourth isoform that shows a Thr substitution for aa 152-595.  Human ER alpha is only 46% aa identical to human ER beta.  Over aa 1-116, human ER alpha shares 85% aa identity with mouse ER alpha.

Specifications

Product Name

Recombinant Human Estrogen Receptor alpha Protein

Sinónimos

Estrogen Receptor alpha | ER-alpha | Estradiol receptor | Nuclear receptor subfamily 3 group A member 1 | ER | Era | ESR | ESRA | ESTRR | NR3A | 17*/654 isoform | 7*/819 2 isoform | 7*/822 isoform | 8*/901 isoform | 8*/941 isoform | DKFZp686N23123 | ER al

Grado

Azide Free, Carrier Free, His Tag

Especificaciones y pureza

Carrier Free, Azide Free, His-Tag, ≥90%(SDS-PAGE)

Concentración de endotoxinas

<1.0 EU/μg

Sistema de expresión

E. coli

Aminoácidos

1-185 aa

Secuencia

MHHHHHHMTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYC

Etiqueta proteínica

N-His

Número de adhesión

P03372

Peso molecular previsto

21.0 kDa

SDS-PAGE

24.8kDa and 47.1 kDa, reducing conditions; 24.8kDa and 47.1 kDa, non-reducing conditions

Tipo de molécula

Protein

Almacenamiento y envío

Forma

Lyophilized

Reconstitución

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 0.5 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Condiciones de almacenamiento de almacenamiento

Store at -20°C,Avoid repeated freezing and thawing

Enviado en

Ice chest + Ice pads

Estabilidad y almacenamiento

Store at -20°C for 1 year. Avoid freeze/thaw cycle.

Imágenes

SDS-PAGE: Recombinant Human Estrogen Receptor alpha protein (rp175926)

Recombinant Human Estrogen Receptor alpha protein (rp175926) - SDS-PAGE
Recombinant Human Estrogen Receptor alpha protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing two bands at 24.8 and 47.1 kDa.

Referencias

1. Junjie Luo, Zhiye Hu, Yuan Xiao, Tongxin Yang, Chune Dong, Jian Huang, Hai-Bing Zhou.  (2017)  Rational design and optimization of selenophenes with basic side chains as novel potent selective estrogen receptor modulators (SERMs) for breast cancer therapy.  MedChemComm,  8  (7): (1485-1497).  [PMID:30108860] [10.1039/C7MD00163K]

2. Yuxuan Dai, Na Yue, Junni Gong, Chunxia Liu, Qifei Li, Jiaqi Zhou, Wenlong Huang, Hai Qian.  (2019)  Development of cell-permeable peptide-based PROTACs targeting estrogen receptor α.  EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY,      [PMID:31865016] [10.1016/j.ejmech.2019.111967]