L6 Whole Cell Lysate: sc-364196

L6 Whole Cell Lysate is derived from the L6 cell line, which originates from rat skeletal muscle tissue. This particular cell line is highly valued in research due to its ability to differentiate into myotubes, making it a powerful model for studying muscle cell biology, specifically muscle development and regeneration. The lysate itself consists of a rich array of cellular components such as proteins, nucleic acids, enzymes, and other metabolic products extracted from disrupted L6 cells. In the realm of research, L6 Whole Cell Lysate has been pivotal in studying the biochemical pathways and regulatory mechanisms involved in muscle protein synthesis, muscle cell response to growth factors, and the effects of various physiochemical conditions on muscle cells. It is frequently used as a standard or control in biochemical assays and protein studies to ensure the accuracy of experimental findings related to muscle physiology. Additionally, this lysate facilitates the exploration of intracellular signaling pathways and the effects of agents on these pathways. Through such applications, L6 Whole Cell Lysate contributes significantly to our understanding of muscle biology and the complex processes governing muscle growth and differentiation.

L6 Whole Cell Lysate References:

1. Dexamethasone inhibits insulin-like growth factor signaling and potentiates myoblast apoptosis.  |  Singleton, JR., et al. 2000. Endocrinology. 141: 2945-50. PMID: 10919283
2. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions.  |  Du, J., et al. 2004. J Clin Invest. 113: 115-23. PMID: 14702115
3. Intracellular ceramide synthesis and protein kinase Czeta activation play an essential role in palmitate-induced insulin resistance in rat L6 skeletal muscle cells.  |  Powell, DJ., et al. 2004. Biochem J. 382: 619-29. PMID: 15193147
4. Identification of molecular target of AMP-activated protein kinase activator by affinity purification and mass spectrometry.  |  Kosaka, T., et al. 2005. Anal Chem. 77: 2050-5. PMID: 15801737
5. Trans-activation of EphA4 and FGF receptors mediated by direct interactions between their cytoplasmic domains.  |  Yokote, H., et al. 2005. Proc Natl Acad Sci U S A. 102: 18866-71. PMID: 16365308
6. Ceramide-activated protein phosphatase involvement in insulin resistance via Akt, serine/arginine-rich protein 40, and ribonucleic acid splicing in L6 skeletal muscle cells.  |  Ghosh, N., et al. 2007. Endocrinology. 148: 1359-66. PMID: 17158207
7. Beneficial effects of beta-sitosterol on glucose and lipid metabolism in L6 myotube cells are mediated by AMP-activated protein kinase.  |  Hwang, SL., et al. 2008. Biochem Biophys Res Commun. 377: 1253-8. PMID: 18992226
8. GAPDH binds GLUT4 reciprocally to hexokinase-II and regulates glucose transport activity.  |  Zaid, H., et al. 2009. Biochem J. 419: 475-84. PMID: 19140804
9. Protection by extra virgin olive oil against oxidative stress in vitro and in vivo. Chemical and biological studies on the health benefits due to a major component of the Mediterranean diet.  |  Rossi, M., et al. 2017. PLoS One. 12: e0189341. PMID: 29283995
10. Estrogen biosynthesis in cultured skeletal muscle cells (L6) induced by amino acids.  |  Iresjö, BM., et al. 2019. Genes Nutr. 14: 29. PMID: 31741685
11. Regulation of hexokinase II gene transcription and glucose phosphorylation by catecholamines, cyclic AMP, and insulin.  |  Osawa, H., et al. 1995. Diabetes. 44: 1426-32. PMID: 7589850
12. Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation.  |  James, SR., et al. 1996. Biochem J. 315 (Pt 3): 709-13. PMID: 8645147
13. Constitutive activation of protein kinase B alpha by membrane targeting promotes glucose and system A amino acid transport, protein synthesis, and inactivation of glycogen synthase kinase 3 in L6 muscle cells.  |  Hajduch, E., et al. 1998. Diabetes. 47: 1006-13. PMID: 9648821