DL-Lysine-[1-13C,epsilon-15N] Dihydrochloride

DL-Lysine-[1-13C,epsilon-15N] Dihydrochloride, a labeled amino acid utilized in diverse research applications, offers unparalleled opportunities for exploration. Here are the key applications:

Stable Isotope Labeling: Immersed in stable isotope labeling experiments, DL-Lysine-[1-13C,epsilon-15N] Dihydrochloride sheds light on protein synthesis and metabolism dynamics. By embedding these isotopic tracers within proteins, researchers embark on a journey to unravel metabolic pathways through the lens of mass spectrometry. This intricate process unveils nuanced details of protein dynamics and turnover rates, offering a profound glimpse into the inner workings of biological systems.

NMR Spectroscopy: Within the domain of nuclear magnetic resonance (NMR) spectroscopy, the labeled DL-Lysine emerges as a cornerstone in elucidating protein structure and interactions. Enriched with 13C and 15N isotopes, it elevates the resolution and sensitivity of NMR signals, facilitating the deciphering of atomic-level intricacies in biomolecular complexes. This capability serves as a vital tool in deciphering the intricate relationship between protein structure and function, unveiling hidden mysteries of cellular processes.

Metabolic Flux Analysis: Venturing into the realm of metabolic flux analysis, researchers leverage DL-Lysine-[1-13C,epsilon-15N] Dihydrochloride to navigate the complexities of cellular metabolism within cultured cells. By tracing the labeled atoms along metabolic pathways, scientists quantify fluxes and gain profound insights into cellular metabolic landscapes. This knowledge forms the bedrock for devising novel metabolic engineering strategies and refining biotechnological processes, ushering in a new era of precision in cellular manipulation.

Proteomics: Within the realm of proteomics, the labeled DL-Lysine emerges as a pivotal tool for accurate quantification and comparative analysis of protein expression levels. It serves as the linchpin for methodologies like SILAC (Stable Isotope Labeling by/with Amino acids in Cell culture), enabling comprehensive exploration of proteomes under diverse conditions. This analytical prowess aids in pinpointing critical biomarkers and unraveling the intricate cellular responses governing health and disease, guiding researchers towards transformative discoveries in the proteomic landscape.