82152-65-6

Basic information

• Product Name: DL-LEUCINE-1-13C
• Synonyms: DL-LEUCINE-1-13C;DL-LEUCINE-1-13C, 99 ATOM % 13C
• CAS NO: 82152-65-6
• Molecular Formula: C6H13NO2
• Molecular Weight: 132.18
• Product Categories: Amino Acids 13C, 2H, 15N;Alphabetical Listings;I-L;Stable Isotopes
• Mol File: 82152-65-6.mol
• Article Data: 6

Chemical Properties

• Melting Point: 293-296 °C (subl.)(lit.)
• Appearance: /
• CAS DataBase Reference: DL-LEUCINE-1-13C(CAS DataBase Reference)
• NIST Chemistry Reference: DL-LEUCINE-1-13C(82152-65-6)
• EPA Substance Registry System: DL-LEUCINE-1-13C(82152-65-6)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 82152-65-6(Hazardous Substances Data)

Usage

General Description

DL-Leucine-1-13C is a stable isotope form of the essential amino acid leucine. It is labeled with a single carbon-13 isotope at the first position of the molecule. This labeling allows for easy detection and quantification using mass spectrometry techniques. DL-Leucine-1-13C is commonly used in metabolic studies and tracer experiments to track the fate and metabolism of leucine in biological systems. Due to its stable isotope labeling, it can also be used for protein turnover studies and flux analysis in various biological and medical research applications.

Upstream product

• 80134-83-4 L-leucine-1-¹³C,¹⁵N 
• 82152-60-1 C₅⁽¹³⁾CH₁₃⁽¹⁵⁾NO₂ 
• 74292-94-7 (1-¹³C)-L-leucine 

Downstream Products

• 125069-90-1 N-Cbz-1-13C-L-leucine 

Relevant articles and documents

Protein quantitative labeling reagent and preparation method and application thereof

The invention provides a protein quantitative labeling reagent as well as a preparation method and application thereof. According to the protein quantitative labeling reagent provided by the invention, the high reaction activity of a o-phthalaldehyde grou

N,N-Dimethyl leucines as novel Isobaric tandem mass tags for quantitative proteomics and peptidomics

Herein, we describe the development and application of a set of novel N,N-dimethyl leucine (DiLeu) 4-plex isobaric tandem mass (MS2) tagging reagents with high quantitation efficacy and greatly reduced cost for neuropeptide and protein analysis. DiLeu reagents serve as attractive alternatives for isobaric tags for relative and absolute quantitation (iTRAQ) and tandem mass tags (TMTs) due to their synthetic simplicity, labeling efficiency, and improved fragmentation efficiency. DiLeu reagent resembles the general structure of a tandem mass tag in that it contains an amine reactive group (triazine ester) targeting the N-terminus and ε-amino group of the lysine side chain of a peptide, a balance group, and a reporter group. A mass shift of 145.1 Da is observed for each incorporated label. Intense a1 reporter ions at m/z 115.1, 116.1, 117.1, and 118.1 are observed for all pooled samples upon MS2. All labeling reagents are readily synthesized from commercially available chemicals with greatly reduced cost Labels 117 and 118 can be synthesized in one step and labels 115 and 116 can be synthesized in two steps. Both DiLeu and iTRAQ reagents show comparable protein sequence coverage (～43%) and quantitation accuracy ( a marine model organism, Callinectes sapidus.

STABLE ISOTOPE-LABELED AMINO ACID, METHOD OF INTEGRATING THE SAME INTO TARGET PROTEIN, METHOD OF NMR STRUCTURAL ANALYSIS OF PROTEIN AND PROCESS FOR PRODUCING SITE-SELECTIVE STABLE ISOTOPE-LABELED FUMARIC ACID AND TARTARIC ACID

The present invention provides a stable isotope-labeled amino acid which is at least one of amino acids constituting a protein and which has at least one of the following labeling patterns:(a) hydrogen atoms except at least one hydrogen atom in one or more methylene groups are deuterated,(b) hydrogen atoms in one of prochiral gem-methyl groups are completely deuterated,(c) hydrogen atoms in prochiral methyl groups are partially deuterated, and(d) all hydrogen atoms except one of them in methyl group are deuterated and hydrogen atoms in the aromatic ring are partially deuterated. With the stable isotope-labeled amino acid, the deuteration of protein can be attained without damaging the NMR sensitivity of remaining hydrogen nucleus and, in addition, the rapid, accurate analysis of NMR spectrum of a high-molecular protein which is beyond the limitation in the prior art and the determination of the stereo-structure can be performed at the same time.