Sp1 Gel Shift Oligonucleotides: sc-2502

Sp1 Gel Shift Oligonucleotides are short sequences of DNA designed for use in gel shift assays, primarily focusing on the study of transcription factor binding. These oligonucleotides are derived from the consensus binding sequence of the Sp1 transcription factor, a zinc finger protein crucial for the regulation of gene expression. Sp1 is involved in the transcriptional activation of numerous genes related to cell growth, differentiation, and apoptosis. By employing Sp1 Gel Shift Oligonucleotides in gel shift assays, researchers can investigate the binding specificity and affinity of Sp1 to its target DNA sequences under various experimental conditions. This technique provides insights into the molecular mechanisms underlying gene regulation mediated by Sp1 and its interactions with other transcriptional regulators. Furthermore, Sp1 Gel Shift Oligonucleotides have been extensively used in research to explain the role of Sp1 in various biological processes, including embryonic development, cancer progression, and cellular response to environmental stressors.

Sp1 Gel Shift Oligonucleotides References:

1. An Sp1 binding site is essential for basal activity of the human prostate-specific transglutaminase gene (TGM4) promoter.  |  Dubbink, HJ., et al. 1999. Gene. 240: 261-7. PMID: 10580145
2. Effects of novel polymorphisms in the RAGE gene on transcriptional regulation and their association with diabetic retinopathy.  |  Hudson, BI., et al. 2001. Diabetes. 50: 1505-11. PMID: 11375354
3. Regulation of the human transforming growth factor beta type II receptor gene promoter by novel Sp1 sites.  |  Jennings, R., et al. 2001. Oncogene. 20: 6899-909. PMID: 11687969
4. Transplacental effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin on the temporal modulation of Sp1 DNA binding in the developing cerebral cortex and cerebellum.  |  Nayyar, T., et al. 2002. Exp Toxicol Pathol. 53: 461-8. PMID: 11926288
5. Functional characterization of transcription factor binding sites for HNF1-alpha, HNF3-beta (FOXA2), HNF4-alpha, Sp1 and Sp3 in the human prothrombin gene enhancer.  |  Ceelie, H., et al. 2003. J Thromb Haemost. 1: 1688-98. PMID: 12911579
6. Glutamine stimulates argininosuccinate synthetase gene expression through cytosolic O-glycosylation of Sp1 in Caco-2 cells.  |  Brasse-Lagnel, C., et al. 2003. J Biol Chem. 278: 52504-10. PMID: 14570901
7. Functional importance of Myc-associated zinc finger protein for the human parathyroid hormone (PTH)/PTH-related peptide receptor-1 P2 promoter constitutive activity.  |  Leroy, C., et al. 2004. J Mol Endocrinol. 32: 99-113. PMID: 14765995
8. The SANT domain of human MI-ER1 interacts with Sp1 to interfere with GC box recognition and repress transcription from its own promoter.  |  Ding, Z., et al. 2004. J Biol Chem. 279: 28009-16. PMID: 15117948
9. Analysis of human UDP-glucose dehydrogenase gene promoter: identification of an Sp1 binding site crucial for the expression of the large transcript.  |  Vatsyayan, J., et al. 2005. J Biochem. 137: 703-9. PMID: 16002992
10. Regulation of human protein Z gene expression by liver-enriched transcription factor HNF-4alpha and ubiquitous factor Sp1.  |  Sugawara, H., et al. 2007. J Thromb Haemost. 5: 2250-8. PMID: 17958743
11. Neuronal nitric oxide synthase interacts with Sp1 through the PDZ domain inhibiting Sp1-mediated copper-zinc superoxide dismutase expression.  |  Baldelli, S., et al. 2011. Int J Biochem Cell Biol. 43: 163-9. PMID: 21056687
12. Transcription factor Sp1 regulates basal transcription of the human DRG2 gene.  |  Kim, HJ., et al. 2011. Biochim Biophys Acta. 1809: 184-90. PMID: 21296692
13. Exposure to inhaled particulate matter activates early markers of oxidative stress, inflammation and unfolded protein response in rat striatum.  |  Guerra, R., et al. 2013. Toxicol Lett. 222: 146-54. PMID: 23892126
14. Bipartite structure of the proximal promoter of a human H4 histone gene.  |  Wright, KL., et al. 1995. J Cell Biochem. 58: 372-9. PMID: 7593258
15. Induction of Sp1 activity by prolactin and interleukin-2 in Nb2 T-cells: differential association of Sp1-DNA complexes with Stats.  |  Too, CK. 1997. Mol Cell Endocrinol. 129: 7-16. PMID: 9175624