LNCaP Cell Lysate: sc-2231

LNCaP Cell Lysate originates from the LNCaP cell line, a human prostate cancer cell line widely used in research to explore prostate cancer biology and oncogenesis. These cells were first derived from a metastatic lesion of human prostatic adenocarcinoma, and the lysate produced from these cells contains a comprehensive mix of proteins, DNA, RNA, and other cellular components, achieved through the lysis of LNCaP cells. This complex biochemical soup provides a snapshot of the cell's molecular environment at the time of lysis, including various cellular signaling pathways and metabolic processes. In research contexts, LNCaP Cell Lysate is primarily utilized to study the behavior of prostate cancer cells at the molecular level. It is particularly useful in proteomics research for identifying protein-protein interactions, protein expression levels, and post-translational modifications specific to prostate cancer cells. Moreover, scientists use this lysate in Western blotting techniques to validate the expression of prostate-specific antigens and other oncogenic markers. This assists in advancing our understanding of the mechanisms driving prostate cancer progression and the cellular impact of genetic or environmental factors on these cells, providing vital insights that support broader research in cellular and molecular oncology.

LNCaP Cell Lysate References:

1. STAT3 mediates IL-6-induced growth inhibition in the human prostate cancer cell line LNCaP.  |  Spiotto, MT. and Chung, TD. 2000. Prostate. 42: 88-98. PMID: 10617865
2. Effect of beta-sitosterol, a plant sterol, on growth, protein phosphatase 2A, and phospholipase D in LNCaP cells.  |  Awad, AB., et al. 2000. Nutr Cancer. 36: 74-8. PMID: 10798219
3. Quercetin inhibits the expression and function of the androgen receptor in LNCaP prostate cancer cells.  |  Xing, N., et al. 2001. Carcinogenesis. 22: 409-14. PMID: 11238180
4. Interleukin-6- and cyclic AMP-mediated signaling potentiates neuroendocrine differentiation of LNCaP prostate tumor cells.  |  Deeble, PD., et al. 2001. Mol Cell Biol. 21: 8471-82. PMID: 11713282
5. The F-box protein SKP2 mediates androgen control of p27 stability in LNCaP human prostate cancer cells.  |  Lu, L., et al. 2002. BMC Cell Biol. 3: 22. PMID: 12188931
6. Curcumin (diferuloyl-methane) enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in LNCaP prostate cancer cells.  |  Deeb, D., et al. 2003. Mol Cancer Ther. 2: 95-103. PMID: 12533677
7. Protease-activated receptor mediated RhoA signaling and cytoskeletal reorganization in LNCaP cells.  |  Greenberg, DL., et al. 2003. Biochemistry. 42: 702-9. PMID: 12534282
8. Role of p53 and NF-kappaB in epigallocatechin-3-gallate-induced apoptosis of LNCaP cells.  |  Hastak, K., et al. 2003. Oncogene. 22: 4851-9. PMID: 12894226
9. Labeling and identification of LNCaP cell surface proteins: a pilot study.  |  Whitaker, HC., et al. 2007. Prostate. 67: 943-54. PMID: 17440980
10. A re-evaluation of LINE-1 ORF2 expression in LNCaP prostate cancer cells.  |  Briggs, EM., et al. 2019. Mob DNA. 10: 51. PMID: 31890047
11. Analysis of glycosylation of prostate-specific membrane antigen derived from LNCaP cells, prostatic carcinoma tumors, and serum from prostate cancer patients.  |  Holmes, EH., et al. 1996. Prostate Suppl. 7: 25-9. PMID: 8950359
12. Location of prostate-specific membrane antigen in the LNCaP prostate carcinoma cell line.  |  Troyer, JK., et al. 1997. Prostate. 30: 232-42. PMID: 9111600
13. Identification, purification, and subcellular localization of prostate-specific membrane antigen PSM′ protein in the LNCaP prostatic carcinoma cell line.  |  Grauer, LS., et al. 1998. Cancer Res. 58: 4787-9. PMID: 9809977