HCT-116 Whole Cell Lysate: sc-364175

HCT-116 whole cell lysate is derived from the HCT-116 cell line, a human colorectal carcinoma model frequently used in cancer research to explore tumor biology and cellular responses to various treatments. This lysate is essential for studying the mechanisms of cell proliferation, apoptosis, and DNA repair in colorectal cancer. Researchers leverage HCT-116 lysate to investigate the signaling pathways implicated in cancer progression, such as Wnt/β-catenine, PI3K/Akt, and MAPK/ERK pathways, which are known to drive tumorigenesis and metastatic potential in colorectal cancer cells. Moreover, HCT-116 cells harbor mutations in key oncogenes and tumor suppressors, including KRAS and TP53, making this lysate particularly useful for examining the effects of these genetic alterations on cellular behavior and drug response. The lysate is employed in proteomic analyses to identify differential protein expression and post-translational modifications, providing insights into the molecular underpinnings of cancer resistance to chemotherapeutic agents and targeted therapies. By using HCT-116 whole cell lysate, scientists can perform comparative studies to understand the differences in signaling dynamics and protein interactions between cancerous and non-cancerous cells. This research contributes to a deeper understanding of colorectal cancer biology and aids in the development of novel strategies for cancer treatment.

HCT-116 Whole Cell Lysate References:

1. 2-D DIGE analysis of butyrate-treated HCT-116 cells after enrichment with heparin affinity chromatography.  |  Tan, HT., et al. 2006. J Proteome Res. 5: 1098-106. PMID: 16674099
2. APM2 is a novel mediator of cisplatin resistance in a variety of cancer cell types regardless of p53 or MMR status.  |  Scott, BJ., et al. 2009. Int J Cancer. 125: 1193-204. PMID: 19444912
3. Creatine kinase brain overexpression protects colorectal cells from various metabolic and non-metabolic stresses.  |  Mooney, SM., et al. 2011. J Cell Biochem. 112: 1066-75. PMID: 21308735
4. Identification of N-terminally truncated stable nuclear isoforms of CDC25B that are specifically involved in G2/M checkpoint recovery.  |  Jullien, D., et al. 2011. Cancer Res. 71: 1968-77. PMID: 21363925
5. Targeting Bax interaction sites reveals that only homo-oligomerization sites are essential for its activation.  |  Peng, R., et al. 2013. Cell Death Differ. 20: 744-54. PMID: 23392123
6. PEA15 regulates the DNA damage-induced cell cycle checkpoint and oncogene-directed transformation.  |  Nagarajan, A., et al. 2014. Mol Cell Biol. 34: 2264-82. PMID: 24710276
7. Ritterostatin GN 1N , a Cephalostatin-Ritterazine Bis-steroidal Pyrazine Hybrid, Selectively Targets GRP78.  |  Ambrose, AJ., et al. 2017. Chembiochem. 18: 506-510. PMID: 28074539
8. Time-dependent shotgun proteomics revealed distinct effects of an organoruthenium prodrug and its activation product on colon carcinoma cells.  |  Meier-Menches, SM., et al. 2019. Metallomics. 11: 118-127. PMID: 30106070
9. Combination therapies induce cancer cell death through the integrated stress response and disturbed pyrimidine metabolism.  |  Hartleben, G., et al. 2021. EMBO Mol Med. 13: e12461. PMID: 33665961
10. Global analysis of RNA-binding proteins identifies a positive feedback loop between LARP1 and MYC that promotes tumorigenesis.  |  Desi, N., et al. 2022. Cell Mol Life Sci. 79: 147. PMID: 35195778
11. Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions.  |  Malki, I., et al. 2022. Nucleic Acids Res. 50: 13045-13062. PMID: 36537190