COLO 320DM Cell Lysate: sc-2226

The COLO 320DM Cell Lysate is produced from the COLO 320DM cell line, a human colorectal carcinoma cell line distinguished by its unique characteristics and adaptations. Originating from a metastatic site, this cell line encapsulates a variety of cellular components, extracted through processes such as sonication, detergent lysis, or enzymatic breakdown, resulting in a lysate rich in proteins, nucleic acids, lipids, and other intracellular molecules. The COLO 320DM Cell Lysate is extensively used in research settings to explore the fundamental aspects of colorectal carcinoma cell biology, focusing on cellular processes like adhesion, motility, and intracellular signaling mechanisms. Researchers utilize this lysate to perform proteomic analyses, enabling the identification and quantification of proteins that play crucial roles in cancer cell physiology and the underlying mechanisms that drive cellular behavior in colorectal cancer. Additionally, it serves as a vital tool in genetic studies, helping to explain gene expression patterns and regulatory networks within these cancer cells. By providing a comprehensive molecular profile, the COLO 320DM Cell Lysate supports advanced research aimed at understanding the complex dynamics of cancer cell biology, contributing significantly to the field of cellular and molecular biology.

COLO 320DM Cell Lysate References:

1. Leptin promotes the proliferative response and invasiveness in human endometrial cancer cells by activating multiple signal-transduction pathways.  |  Sharma, D., et al. 2006. Endocr Relat Cancer. 13: 629-40. PMID: 16728588
2. Leptin stimulates proliferation and inhibits apoptosis in Barrett′s esophageal adenocarcinoma cells by cyclooxygenase-2-dependent, prostaglandin-E2-mediated transactivation of the epidermal growth factor receptor and c-Jun NH2-terminal kinase activation.  |  Ogunwobi, O., et al. 2006. Endocrinology. 147: 4505-16. PMID: 16740977
3. Indirect effects of leptin receptor deficiency on lymphocyte populations and immune response in db/db mice.  |  Palmer, G., et al. 2006. J Immunol. 177: 2899-907. PMID: 16920925
4. leptin-induced growth stimulation of breast cancer cells involves recruitment of histone acetyltransferases and mediator complex to CYCLIN D1 promoter via activation of Stat3.  |  Saxena, NK., et al. 2007. J Biol Chem. 282: 13316-25. PMID: 17344214
5. Concomitant activation of the JAK/STAT, PI3K/AKT, and ERK signaling is involved in leptin-mediated promotion of invasion and migration of hepatocellular carcinoma cells.  |  Saxena, NK., et al. 2007. Cancer Res. 67: 2497-507. PMID: 17363567
6. Leptin synergistically enhances the anti-apoptotic and growth-promoting effects of acid in OE33 oesophageal adenocarcinoma cells in culture.  |  Beales, IL. and Ogunwobi, OO. 2007. Mol Cell Endocrinol. 274: 60-8. PMID: 17618045
7. The intermediate-conductance calcium-activated potassium channel KCa3.1 contributes to atherogenesis in mice and humans.  |  Toyama, K., et al. 2008. J Clin Invest. 118: 3025-37. PMID: 18688283
8. Peculiar antibody reactivity to human connexin 37 and its microbial mimics in patients with Crohn′s disease.  |  Koutsoumpas, A., et al. 2011. J Crohns Colitis. 5: 101-9. PMID: 21453878
9. The intermediate conductance calcium-activated potassium channel KCa3.1 regulates vascular smooth muscle cell proliferation via controlling calcium-dependent signaling.  |  Bi, D., et al. 2013. J Biol Chem. 288: 15843-53. PMID: 23609438
10. Leptin inhibits the Na(+)/K(+) ATPase in Caco-2 cells via PKC and p38MAPK.  |  El-Zein, O., et al. 2015. Cell Signal. 27: 416-23. PMID: 25499980
11. Leptin Inhibits the Apoptosis of Endometrial Carcinoma Cells Through Activation of the Nuclear Factor κB-inducing Kinase/IκB Kinase Pathway.  |  Zhou, X., et al. 2015. Int J Gynecol Cancer. 25: 770-8. PMID: 25811593