MDCK Cell Lysate: sc-2252

MDCK (Madin-Darby Canine Kidney) cell lysate is derived from a canine kidney epithelial cell line widely used in biological research to study cellular processes such as polarity, ion transport, and virus-host interactions. The lysate is particularly valuable for its role in investigating the mechanisms of epithelial barrier function and transport properties, which are essential for understanding fluid and electrolyte balance in tissues. Researchers utilize MDCK cell lysate in studies of transcellular and paracellular transport mechanisms, analyzing the role of tight junction proteins like claudins and occludins. This lysate also serves as a model for studying viral entry, replication, and pathogenesis, especially for influenza and coronavirus, providing insights into how viruses exploit host cellular machinery for their lifecycle. In addition, the MDCK lysate has been instrumental in the development of advanced drug delivery systems, where it is used to assess the permeability of pharmaceutical compounds across epithelial barriers. By providing a consistent and reproducible model, MDCK cell lysate aids in elucidating complex signaling pathways and cellular behaviors, enhancing our understanding of kidney and epithelial cell function strictly within research environments.

MDCK Cell Lysate References:

1. Antibodies differentiate desmosome-form and nucleus-form pinin: evidence that pinin is a moonlighting protein with dual location at the desmosome and within the nucleus.  |  Ouyang, P. 1999. Biochem Biophys Res Commun. 263: 192-200. PMID: 10486276
2. Characterization of thiol-, aspartyl-, and thiol-metallo-peptidase activities in Madin-Darby canine kidney cells.  |  Oliveira, V., et al. 2000. J Cell Biochem. 76: 478-88. PMID: 10649444
3. Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb.  |  Plant, PJ., et al. 2000. J Cell Biol. 149: 1473-84. PMID: 10871286
4. Binding of scatter factor to epithelial cell membrane protein: identification of its receptor.  |  Joseph, A., et al. 1992. Biochim Biophys Acta. 1105: 141-7. PMID: 1314668
5. Cloning and assessment of tumorigenicity and oncogenicity of a Madin-Darby canine kidney (MDCK) cell line for influenza vaccine production.  |  Liu, J., et al. 2010. Vaccine. 28: 1285-93. PMID: 19944150
6. Improved sensitivity of influenza A antigen detection using a combined NP, M, and NS1 sandwich ELISA.  |  Jian-umpunkul, P., et al. 2012. J Virol Methods. 185: 24-31. PMID: 22677225
7. Characterization of cytopathogenicity of classical swine fever virus isolate induced by Newcastle disease virus.  |  Raut, SD., et al. 2015. Virusdisease. 26: 70-6. PMID: 26436124
8. Endogenous RNase inhibitor contributes to stability of RNA in crude cell lysates: Applicability to RT-qPCR.  |  Wang, X., et al. 2016. Anal Biochem. 513: 21-27. PMID: 27544650
9. Induction of a 5-lipoxygenase product by daidzein is involved in the regulation of influenza virus replication.  |  Horio, Y., et al. 2020. J Clin Biochem Nutr. 66: 36-42. PMID: 32001954
10. Evaluation of manufacturing feasibility and safety of an MDCK cell-based live attenuated influenza vaccine (LAIV) platform.  |  Ganguly, M., et al. 2020. Vaccine. 38: 8379-8386. PMID: 33229107
11. Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex.  |  Jou, TS., et al. 1995. Proc Natl Acad Sci U S A. 92: 5067-71. PMID: 7761449
12. Loss of MDCK cell alpha 2 beta 1 integrin expression results in reduced cyst formation, failure of hepatocyte growth factor/scatter factor-induced branching morphogenesis, and increased apoptosis.  |  Saelman, EU., et al. 1995. J Cell Sci. 108 (Pt 11): 3531-40. PMID: 8586664
13. Caveolin-1 and -2 in the exocytic pathway of MDCK cells.  |  Scheiffele, P., et al. 1998. J Cell Biol. 140: 795-806. PMID: 9472032