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L-Histidine-[ring-15N2]

General Information
Catalog: BLP-009031
Molecular Formula: C6H9N[15N]2O2
Molecular Weight: 157.15
Chemical Structure
L-Histidine-[ring-15N2]
Description L-Histidine-[ring-15N2] is the labelled analogue of L-Histidine. L-Histidine is an essential amino acid. It is used as a cell culture media component for the commercial biomanufacture of therapeutic recombinant proteins and monoclonal antibodies.
IUPAC Name L-histidine-Np,Nt-15N2
Related CAS 71-00-1 (unlabelled)
Purity 98% by CP; 98% atom 15N
Storage Store at -20°C

L-Histidine-[ring-15N2] is a labeled amino acid used extensively in bioscience research, particularly in studies involving protein structure and metabolism. Here are some key applications of L-Histidine-[ring-15N2]:

NMR Spectroscopy: L-Histidine-[ring-15N2] is widely employed in Nuclear Magnetic Resonance (NMR) spectroscopy to investigate protein structure and dynamics. The nitrogen isotopic labeling provides distinct resonance signals that facilitate the detailed analysis of histidine residues within proteins. This technique is invaluable for understanding protein folding, conformational changes, and interaction mechanisms.

Metabolic Tracing: The isotopic labeling of L-Histidine-[ring-15N2] makes it an essential tool for metabolic tracing studies. Researchers can track the fate of histidine in metabolic pathways, quantifying its incorporation into proteins and other biomolecules. This information helps in elucidating metabolic fluxes and the regulation of amino acid utilization in various cellular processes.

Enzyme Mechanism Studies: L-Histidine-[ring-15N2] is used to probe enzyme mechanisms, particularly those involving histidine residues in the active site. By incorporating this labeled amino acid, scientists can follow the isotopic shifts during catalysis through techniques like mass spectrometry. This approach helps in revealing detailed insights into enzyme catalysis and the role of histidine in enzymatic reactions.

Protein-Ligand Interaction Studies: L-Histidine-[ring-15N2] can be incorporated into proteins to study their interactions with ligands or other macromolecules. The resulting isotopic label acts as a marker in binding studies, allowing researchers to monitor and quantify binding events using techniques such as Isothermal Titration Calorimetry (ITC) or Surface Plasmon Resonance (SPR). These studies are crucial for drug discovery and the development of therapeutic agents.

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