Date published: 2025-9-18

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ER Gel Shift Oligonucleotides: sc-2585

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Datasheets
  • consensus binding site for ER transcription factor; supplied as 500 ng double-stranded DNA; sc-2585
  • also available as mutant oligonucleotide with "GT"→"TA" substitution in the ER binding site; sc-2586
  • 5′-GGA TCT AGG TCA CTG TGA CCC CGG ATC-3′

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SEE ALSO...

ER Gel Shift Oligonucleotides are short DNA sequences meticulously crafted for application in gel shift assays, a foundational technique in molecular biology research for investigating protein-DNA interactions. The designation "ER" corresponds to the estrogen receptor (ER), a pivotal transcription factor belonging to the nuclear receptor superfamily. ER plays a crucial role in mediating the biological effects of estrogen hormones, regulating gene expression essential in reproductive function, development, and homeostasis. Upon activation by estrogen ligands, ER translocates to the nucleus and binds to specific DNA sequences, known as estrogen response elements (EREs), within the promoters of target genes, thereby modulating their transcriptional activity. By employing ER Gel Shift Oligonucleotides in gel shift assays, researchers explore the binding kinetics, specificity, and affinity of ER to its target DNA sequences under varied experimental conditions. This method facilitates the elucidation of the molecular mechanisms underlying ER-mediated gene regulation and provides insights into the signaling networks governing cellular responses to estrogen signaling.

ER Gel Shift Oligonucleotides References:

  1. DUSP22/LMW-DSP2 regulates estrogen receptor-alpha-mediated signaling through dephosphorylation of Ser-118.  |  Sekine, Y., et al. 2007. Oncogene. 26: 6038-49. PMID: 17384676
  2. The induction of apoptosis by a newly synthesized diosgenyl saponin through the suppression of estrogen receptor-α in MCF-7 human breast cancer cells.  |  Chun, J., et al. 2014. Arch Pharm Res. 37: 1477-86. PMID: 24263408
  3. Identification of authentic estrogen receptor in cultured endothelial cells. A potential mechanism for steroid hormone regulation of endothelial function.  |  Venkov, CD., et al. 1996. Circulation. 94: 727-33. PMID: 8772695

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

ER consensus oligonucleotide

sc-2585
500 ng/25 µl
$49.00

ER mutant oligonucleotide

sc-2586
500 ng/25 µl
$49.00