Jurkat nuclear extract: sc-2132

Jurkat nuclear extract is derived from the Jurkat cell line, a human T lymphocyte line widely used to study T-cell signaling and function. This extract is rich in transcription factors, nuclear enzymes, and signaling molecules, providing a crucial tool for dissecting nuclear events in T-cell activation and regulation. Researchers use Jurkat nuclear extract to investigate the intricacies of transcriptional regulation in T-cells, including how transcription factors like NF-κB and AP-1 are activated following T-cell receptor (TCR) engagement. The extract is employed in a variety of assays such as chromatin immunoprecipitation (ChIP) to explore the binding of transcription factors to DNA in response to different stimuli, and electrophoretic mobility shift assays (EMSA) to assess changes in DNA-binding protein activity. Additionally, it facilitates the study of RNA polymerase activity and the assembly of transcription complexes, providing insights into gene expression changes during T-cell activation. These research applications are purely focused on basic scientific inquiry, aiming to understand cellular signaling pathways and transcriptional networks. The origin and preparation of the Jurkat nuclear extract are carefully controlled to ensure high fidelity and reproducibility in research outcomes.

Jurkat nuclear extract References:

1. Repression of CD2 gene expression is mediated by an AP-2 related factor.  |  Outram, SV., et al. 2001. Biochem Biophys Res Commun. 281: 409-15. PMID: 11181063
2. YY1 and NF-Y binding sites regulate the transcriptional activity of the dek and dek-can promoter.  |  Sitwala, KV., et al. 2002. Oncogene. 21: 8862-70. PMID: 12483538
3. A promoter polymorphism in the central MHC gene, IKBL, influences the binding of transcription factors USF1 and E47 on disease-associated haplotypes.  |  Boodhoo, A., et al. 2004. Gene Expr. 12: 1-11. PMID: 15473256
4. Aldosterone impairs vascular endothelial cell function.  |  Hashikabe, Y., et al. 2006. J Cardiovasc Pharmacol. 47: 609-13. PMID: 16680076
5. Biotinylated probes in the electrophoretic mobility shift assay to examine specific dsDNA, ssDNA or RNA-protein interactions.  |  Ludwig, LB., et al. 1995. Nucleic Acids Res. 23: 3792-3. PMID: 7479014
6. DNA loops induced by cooperative binding of transcriptional activator proteins and preinitiation complexes.  |  Becker, JC., et al. 1995. Proc Natl Acad Sci U S A. 92: 9727-31. PMID: 7568206
7. Multi-strand binding of nuclear factors to a repressor of mouse mammary tumor virus transcription can be distinguished kinetically.  |  Rodda, DJ., et al. 1995. Biochem Biophys Res Commun. 209: 379-84. PMID: 7726860
8. Characterization of NF(P), the nuclear factor that interacts with the regulatory P sequence (5′-CGAAAATTTCC-3′) of the human interleukin-4 gene: relationship to NF-kappa B and NF-AT.  |  Matsuda, I., et al. 1994. Biochem Biophys Res Commun. 199: 439-46. PMID: 8135784
9. Binding of the ubiquitous nuclear transcription factor YY1 to a cis regulatory sequence in the human LINE-1 transposable element.  |  Becker, KG., et al. 1993. Hum Mol Genet. 2: 1697-702. PMID: 8268924
10. Activation of the human vimentin gene by the Tax human T-cell leukemia virus. I. Mechanisms of regulation by the NF-kappa B transcription factor.  |  Lilienbaum, A. and Paulin, D. 1993. J Biol Chem. 268: 2180-8. PMID: 8420985
11. The pancreatic islet factor STF-1 binds cooperatively with Pbx to a regulatory element in the somatostatin promoter: importance of the FPWMK motif and of the homeodomain.  |  Peers, B., et al. 1995. Mol Cell Biol. 15: 7091-7. PMID: 8524276
12. Sp family members preferentially interact with the promoter proximal repeat within the HTLV-I enhancer.  |  Wessner, R., et al. 1997. Leukemia. 11 Suppl 3: 10-3. PMID: 9209281
13. Retinoblastoma protein recruits histone deacetylase to repress transcription.  |  Brehm, A., et al. 1998. Nature. 391: 597-601. PMID: 9468139