p53 Gel Shift Oligonucleotides are short DNA sequences specifically synthesized for application in gel shift assays, a fundamental technique in molecular biology research aimed at exploring protein-DNA interactions. The designation "p53" refers to the tumor suppressor protein p53, a critical transcription factor involved in regulating cellular responses to various stresses, including DNA damage, oxidative stress, and oncogenic signaling. Upon activation by stress signals, p53 translocates to the nucleus and binds to specific DNA sequences, known as p53 response elements (p53REs), within the promoters of target genes, thereby modulating their transcriptional activity and influencing cell fate decisions such as cell cycle arrest, DNA repair, or apoptosis. By utilizing p53 Gel Shift Oligonucleotides in gel shift assays, researchers investigate the binding kinetics, specificity, and affinity of p53 to its target DNA sequences under various experimental conditions. This technique enables the elucidation of the molecular mechanisms underlying p53-mediated gene regulation and provides insights into the complex signaling networks governing cellular responses to stress.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA
LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences
p53 Gel Shift Oligonucleotides References:
- p53 regulates the expression of the tumor suppressor gene maspin. | Zou, Z., et al. 2000. J Biol Chem. 275: 6051-4. PMID: 10692390
- Identification and characterization of a p53 homologue in Drosophila melanogaster. | Jin, S., et al. 2000. Proc Natl Acad Sci U S A. 97: 7301-6. PMID: 10860994
- Direct interaction of p53 with the Y-box binding protein, YB-1: a mechanism for regulation of human gene expression. | Okamoto, T., et al. 2000. Oncogene. 19: 6194-202. PMID: 11175333
- Knock-in mice with a chimeric human/murine p53 gene develop normally and show wild-type p53 responses to DNA damaging agents: a new biomedical research tool. | Luo, JL., et al. 2001. Oncogene. 20: 320-8. PMID: 11313961
- A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis. | Nelson, V., et al. 2001. Apoptosis. 6: 221-34. PMID: 11388671
- Binding of RNA to p53 regulates its oligomerization and DNA-binding activity. | Yoshida, Y., et al. 2004. Oncogene. 23: 4371-9. PMID: 15064727
- Derivation of the consensus DNA-binding sequence for p63 reveals unique requirements that are distinct from p53. | Ortt, K. and Sinha, S. 2006. FEBS Lett. 580: 4544-50. PMID: 16870177
- In vitro analysis of DNA-protein interactions by proximity ligation. | Gustafsdottir, SM., et al. 2007. Proc Natl Acad Sci U S A. 104: 3067-72. PMID: 17360610
- The carboxyl-terminal domain of the p53 protein regulates sequence-specific DNA binding through its nonspecific nucleic acid-binding activity. | Bayle, JH., et al. 1995. Proc Natl Acad Sci U S A. 92: 5729-33. PMID: 7777576
- Dominant negative effect of a germ-line mutant p53: a step fostering tumorigenesis. | Srivastava, S., et al. 1993. Cancer Res. 53: 4452-5. PMID: 8402611
- Antisense p53 provokes changes in HeLa cell growth and morphology. | Iotsova, V. and Stehelin, D. 1995. Eur J Cell Biol. 68: 122-32. PMID: 8575459
- Human smooth muscle alpha-actin gene is a transcriptional target of the p53 tumor suppressor protein. | Comer, KA., et al. 1998. Oncogene. 16: 1299-308. PMID: 9546431
- Specificin VitroBinding of p53 to the Promoter Region of the Human Mismatch Repair Gene hMSH2. | Scherer, S. J., Welter, C., Zang, K. D., & Dooley, S. (1996. Biochemical and biophysical research communications,. 221(3),: 722-728.