L-Leucine-[1,2-13C2]

L-Leucine-[1,2-13C2], a stable isotope-labeled amino acid, is widely utilized in various research applications. Here are the key applications of L-Leucine-[1,2-13C2]:

Metabolic Flux Analysis: Researchers delve into metabolic flux analysis, leveraging L-Leucine-[1,2-13C2] to meticulously trace the intricate pathways of leucine’s incorporation and utilization within metabolic networks. By utilizing mass spectrometry, scientists can scrutinize the fate of labeled carbon atoms, tracking the fluxes of metabolism across diverse biological systems. This methodological approach is paramount for unraveling the complexities of amino acid metabolism, protein synthesis, and degradation pathways.

Protein Turnover Studies: In the realm of protein turnover studies, L-Leucine-[1,2-13C2] emerges as a pivotal tracer, enabling the quantification of protein synthesis and degradation rates in cellular and tissue contexts. By integrating this isotopically labeled amino acid into newly synthesized proteins, researchers can precisely measure protein turnover using cutting-edge techniques like mass spectrometry and nuclear magnetic resonance (NMR). This information serves as a linchpin for investigating muscle physiology, aging processes, and pathological conditions characterized by aberrant protein metabolism.

Nutritional Research: Within the domain of nutritional research, L-Leucine-[1,2-13C2] plays a crucial role in facilitating investigations into the dynamic kinetics of amino acid absorption, transport, and utilization within living organisms. By evaluating how diverse dietary regimens or supplements impact leucine metabolism, scientists can craft tailored nutritional strategies aimed at enhancing health and performance outcomes. This labeled amino acid serves as a vital tool for precisely delineating dietary leucine requirements and unraveling its metabolic destiny.

Isotopic Labeling in Proteomics: Integrated within the framework of proteomics, L-Leucine-[1,2-13C2] is strategically deployed for isotopic labeling purposes in quantitative protein studies. By employing the renowned technique of stable isotope labeling by amino acids in cell culture (SILAC), researchers can achieve meticulous quantification of protein expression levels and post-translational modifications. This methodology enables comparative analyses of protein dynamics under diverse experimental conditions, offering profound insights into cellular responses and the underlying mechanisms of disease states.