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L-LEUCINE-D3-N-FMOC (METHYL-D3), also known as Fmoc-Leu-OH-5,5,5-d3, is an isotope-labeled compound of Fmoc-L-Leu-OH (F625015). It is an amino acid derivative used in peptide chemistry and has potential applications in various fields due to its unique properties.

538372-74-6

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538372-74-6 Usage

Uses

Used in Pharmaceutical Industry:
L-LEUCINE-D3-N-FMOC (METHYL-D3) is used as a novel PPARγ ligand for activating PPARγ in different ways. This activation helps reduce osteoclast differentiation, making it a better therapeutic target in diabetes management compared to traditional antidiabetic drugs.
Used in Peptide Chemistry:
L-LEUCINE-D3-N-FMOC (METHYL-D3) is used as an amino acid derivative in peptide chemistry, allowing for the synthesis of various peptides with potential applications in research and drug development.

Check Digit Verification of cas no

The CAS Registry Mumber 538372-74-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 5,3,8,3,7 and 2 respectively; the second part has 2 digits, 7 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 538372-74:
(8*5)+(7*3)+(6*8)+(5*3)+(4*7)+(3*2)+(2*7)+(1*4)=176
176 % 10 = 6
So 538372-74-6 is a valid CAS Registry Number.

538372-74-6SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name (((9H-fluoren-9-yl)methoxy)carbonyl)-L-leucine-5,5,5-d3

1.2 Other means of identification

Product number -
Other names -

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:538372-74-6 SDS

538372-74-6Downstream Products

538372-74-6Relevant academic research and scientific papers

CycLS: Accurate, whole-library sequencing of cyclic peptides using tandem mass spectrometry

Townsend, Chad,Furukawa, Akihiro,Schwochert, Joshua,Pye, Cameron R.,Edmondson, Quinn,Lokey, R. Scott

supporting information, p. 1232 - 1238 (2018/02/21)

Cyclic peptides are of great interest as therapeutic compounds due to their potential for specificity and intracellular activity, but specific compounds can be difficult to identify from large libraries without resorting to molecular encoding techniques. Large libraries of cyclic peptides are often DNA-encoded or linearized before sequencing, but both of those deconvolution strategies constrain the chemistry, assays, and quantification methods which can be used. We developed an automated sequencing program, CycLS, to identify cyclic peptides contained within large synthetic libraries. CycLS facilitates quick and easy identification of all library-members via tandem mass spectrometry data without requiring any specific chemical moieties or modifications within the library. Validation of CycLS against a library of 400 cyclic hexapeptide peptoid hybrids (peptomers) of unique mass yielded a result of 95% accuracy when compared against a simulated library size of 234,256 compounds. CycLS was also evaluated by resynthesizing pure compounds from a separate 1800-member library of cyclic hexapeptides and hexapeptomers with high mass redundancy. Of 22 peptides resynthesized, 17 recapitulated the retention times and fragmentation patterns assigned to them from the whole-library bulk assay results. Implementing a database-matching approach, CycLS is fast and provides a robust method for sequencing cyclic peptides that is particularly applicable to the deconvolution of synthetic libraries.

Improved CILAT reagents for quantitative proteomics

Zeng, Dexing,Li, Shuwei

supporting information; experimental part, p. 2059 - 2061 (2009/12/03)

Improved CILAT reagents have been developed, with which an unprecedented number of protein samples can be measured in high-throughput assays, providing a robust tool for MS-based quantitative proteomics.

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