ZR-75-1 Cell Lysate: sc-2241

ZR-75-1 Cell Lysate, derived from a human breast cancer cell line, is utilized extensively in scientific research to study signaling pathways and molecular mechanisms of cancer. The lysate contains a complex mixture of proteins, nucleic acids, and other cellular components that are instrumental in elucidating the role of various oncogenes and tumor suppressors. One primary application involves the analysis of the PI3K/AKT/mTOR pathway, critical in regulating cell growth and survival. Researchers use ZR-75-1 Cell Lysate to investigate the activation states of key proteins within this pathway via techniques like western blotting and mass spectrometry. Additionally, it serves as a model to study hormone receptor signaling, particularly estrogen receptor (ER) and progesterone receptor (PR) pathways, given the cell line's hormone responsiveness. This lysate is also valuable in examining the effects of chemical inhibitors and activators on cellular processes, such as apoptosis, proliferation, and migration. By using ZR-75-1 Cell Lysate, scientists can explore the complex network of signaling events that drive cancer progression and identify potential biomarkers for disease states. Its diverse applications in research underscore its importance in advancing our understanding of cellular mechanisms in oncology.

ZR-75-1 Cell Lysate References:

1. The differential processing of proenkephalin A in mouse and human breast tumour cell lines.  |  Brar, BK. and Lowry, PJ. 1999. J Endocrinol. 161: 475-84. PMID: 10333550
2. Human DF3/MUC1 carcinoma-associated protein functions as an oncogene.  |  Li, Y., et al. 2003. Oncogene. 22: 6107-10. PMID: 12955090
3. Fatty acid synthase as a tumor marker: its extracellular expression in human breast cancer.  |  Wang, YY., et al. 2004. J Exp Ther Oncol. 4: 101-10. PMID: 15500005
4. Arylamine N-acetyltransferase 1 expression in breast cancer cell lines: a potential marker in estrogen receptor-positive tumors.  |  Wakefield, L., et al. 2008. Genes Chromosomes Cancer. 47: 118-26. PMID: 17973251
5. Selective small molecule inhibitors of the potential breast cancer marker, human arylamine N-acetyltransferase 1, and its murine homologue, mouse arylamine N-acetyltransferase 2.  |  Russell, AJ., et al. 2009. Bioorg Med Chem. 17: 905-18. PMID: 19059786
6. Expression of A disintegrin and metalloprotease 10 in pancreatic carcinoma.  |  Gaida, MM., et al. 2010. Int J Mol Med. 26: 281-8. PMID: 20596609
7. Ontogenesis of Ap-2γ expression in rat testes.  |  Hou, M., et al. 2011. Sex Dev. 5: 188-96. PMID: 21654158
8. Selectin ligand sialyl-Lewis x antigen drives metastasis of hormone-dependent breast cancers.  |  Julien, S., et al. 2011. Cancer Res. 71: 7683-93. PMID: 22025563
9. MUC1-C oncoprotein regulates glycolysis and pyruvate kinase M2 activity in cancer cells.  |  Kosugi, M., et al. 2011. PLoS One. 6: e28234. PMID: 22140559
10. Arylamine N-acetyltransferases--from drug metabolism and pharmacogenetics to identification of novel targets for pharmacological intervention.  |  Sim, E., et al. 2012. Adv Pharmacol. 63: 169-205. PMID: 22776642
11. Structure-activity relationships and colorimetric properties of specific probes for the putative cancer biomarker human arylamine N-acetyltransferase 1.  |  Egleton, JE., et al. 2014. Bioorg Med Chem. 22: 3030-54. PMID: 24758871
12. A novel function of HER2/Neu in the activation of G2/M checkpoint in response to γ-irradiation.  |  Yan, Y., et al. 2015. Oncogene. 34: 2215-26. PMID: 24909175
13. Complexity of MAM-6, an epithelial sialomucin associated with carcinomas.  |  Hilkens, J., et al. 1989. Cancer Res. 49: 786-93. PMID: 2643463
14. Galectin-1 Influences Breast Cancer Cell Adhesion to E-selectin Via Ligand Intermediaries.  |  Reynolds, NM., et al. 2018. Cell Mol Bioeng. 11: 37-52. PMID: 31719877
15. Identification of cancer protein biomarker based on cell specific peptide and its potential role in predicting tumor metastasis.  |  Li, L., et al. 2023. J Proteomics. 275: 104826. PMID: 36708809