D-Lysine-[4,4,5,5-d4] hydrochloride

D-Lysine-[4,4,5,5-d4] hydrochloride, a labeled amino acid of significance in scientific research, finds diverse applications in various domains. Here are the key applications:

Stable Isotope Labeling: In the realm of quantitative proteomics, the utilization of D-Lysine-[4,4,5,5-d4] hydrochloride for stable isotope labeling stands as a cornerstone. By integrating this uniquely labeled lysine into proteins, scientists embark on a journey of precise quantification of protein expression levels using the powerful tool of mass spectrometry. This endeavor not only facilitates a deeper understanding of protein function but also unveils potential biomarker candidates for a myriad of diseases, thereby illuminating new paths in the domain of medical research.

Metabolic Tracing: Within the intricate realm of metabolic studies, the application of D-Lysine-[4,4,5,5-d4] emerges as a beacon for tracing the metabolic pathways of lysine incorporation and degradation. Researchers delve into the intricate dance of labeled lysine within cellular metabolism, unraveling insights into amino acid dynamics and metabolic fluxes. This exploration serves as a pivotal cornerstone in broadening our comprehension of metabolic disorders and in paving the way for innovative metabolic therapies, ushering in a new era of medical advancements.

Pharmacokinetics: Embarking on a journey into the pharmacokinetics universe, D-Lysine-[4,4,5,5-d4] hydrochloride plays a vital role in the study of drugs interacting with lysine residues. Through the strategic labeling of lysine, researchers embark on a voyage to monitor the absorption, distribution, metabolism, and excretion (ADME) of lysine-conjugated drugs. This critical information becomes the key to optimizing drug design and dosing regimens, unlocking new avenues in pharmaceutical research and development.

Protein-Protein Interactions: Venturing into the intricate world of protein-protein interactions, the labeled D-Lysine-[4,4,5,5-d4] emerges as a pivotal tool for conducting crosslinking experiments. By ingeniously integrating the labeled amino acid into proteins, the realm of mass spectrometry stands ready to reveal interaction sites and conformational alterations. This endeavor sheds light on the mechanisms underpinning protein complexes and their indispensable roles in cellular functions, offering a profound understanding of the intricate dance of proteins within biological systems.