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L-Histidine-[ring-pi-15N]

General Information
Catalog: BLP-009032
Molecular Formula: C6H9N2[15N]O2
Molecular Weight: 156.15
Chemical Structure
L-Histidine-[ring-pi-15N]
Description L-Histidine-[ring-pi-15N] 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-15N
Related CAS 71-00-1 (unlabelled)
Purity 98% by CP; 98% atom 15N
Storage Store at -20°C

L-Histidine-[ring-pi-15N] is an isotopically labeled amino acid used in various biochemical and biophysical studies. Here are some key applications of L-Histidine-[ring-pi-15N]:

NMR Spectroscopy Studies: L-Histidine-[ring-pi-15N] is commonly used in nuclear magnetic resonance (NMR) spectroscopy to study protein structure and dynamics. The isotopic labeling allows for precise resonance assignment and structural elucidation of histidine-containing proteins. This can result in a deeper understanding of protein folding, interactions, and functions.

Enzyme Mechanism Research: This labeled compound is valuable in studying enzyme mechanisms, especially those involving histidine residues in their active sites. By tracking the 15N-label, researchers can gain insights into enzyme-substrate interactions and catalytic mechanisms. This information is crucial for designing enzyme inhibitors and developing therapeutic agents.

Metabolic Flux Analysis: In metabolic studies, L-Histidine-[ring-pi-15N] can be used to trace the metabolic pathways involving histidine. The incorporation of the 15N-label allows for the detailed monitoring of metabolic intermediates and product formation. This helps in understanding cellular metabolism and optimizing metabolic engineering strategies.

Structural Biology: L-Histidine-[ring-pi-15N] is also used in X-ray crystallography and other structural biology techniques to stabilize and identify histidine residues in protein structures. The isotopic label can enhance the resolution and accuracy of structural data. This aids in the development of protein models and the understanding of molecular interactions.

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