201004-29-7

Basic information

• Product Name: FMOC-LYS(ME3)-OH HCL
• Synonyms: FMOC-LYSINE(ME)3-OH CHLORIDE;FMOC-LYS(ME)3-OH CHLORIDE;FMOC-LYS(ME3)-OH HCL;FMOC-N-EPSILON-(TRIMETHYL)-L-LYSINE CHLORIDE;FMOC-L-LYS(ME3)-OH CL;N-ALPHA-FMOC-N-EPSILON,EPSILON,EPSILON-TRIMETHYL-L-LYSINE CHLORIDE;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-N-EPSILON-TRIMETHYLAMONIUM-L-LYSINE CHLORIDE;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-N-EPSILON,N-EPSILON,N-EPSILON-TRIMETHYL-L-LYSINE CHLORIDE
• CAS NO: 201004-29-7
• Molecular Formula: C24H31N2O4.Cl
• Molecular Weight: 446.97
• Product Categories: amino;amino acids
• Mol File: 201004-29-7.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: FMOC-LYS(ME3)-OH HCL(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-LYS(ME3)-OH HCL(201004-29-7)
• EPA Substance Registry System: FMOC-LYS(ME3)-OH HCL(201004-29-7)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 201004-29-7(Hazardous Substances Data)

Usage

Uses

Used in Peptide Synthesis:
FMOC-LYS(ME3)-OH HCL is used as a protected amino acid in peptide synthesis for the incorporation of N-trimethyl lysine residues into peptide sequences. Its protection allows for selective deprotection and coupling during the synthesis process, facilitating the creation of complex peptide structures.
Used in Bioconjugation:
FMOC-LYS(ME3)-OH HCL is used as a building block in the synthesis of peptide linkers for monoclonal antibody-drug conjugates, such as monoclonal antibody-auristatin F conjugates. These conjugates are designed to deliver potent drugs specifically to cancer cells, improving the therapeutic index and reducing side effects.
Used in Analytical Chemistry:
FMOC-LYS(ME3)-OH HCL is used as a component in the preparation of multifunctional reagents with enhanced ionization properties. These reagents are employed for the analysis of protein modifications in human cells and dynamic profiling of protein lipidation, aiding in the study of cellular processes and disease mechanisms.
Used in Protein Synthesis:
FMOC-LYS(ME3)-OH HCL is utilized in sequential peptide ligation techniques to synthesize modified proteins, such as histone H3 containing a trimethyl lysine residue with a modified tail region. This allows for the investigation of the role of specific protein modifications in chromatin structure and function, as well as their implications in various biological processes and diseases.

Upstream product

• 65671-53-6 N²-(tert-butoxycarbonyl)-N⁶,N⁶-dimethyl-L-lysine 
• 1395226-01-3 C₁₄H₂₉N₂O₄⁽¹⁺⁾*Cl^(1-) 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1395226-03-5 C₉H₂₁N₂O₂⁽¹⁺⁾*C₂HF₃O₂*C₂F₃O₂^(1-) 
• 139262-23-0 9-fluorenylmethoxycarbonyl-L-alanine hydrochloride 
• 74-88-4 methyl iodide 
• 252049-10-8 Nα-Fmoc-Nε-dimethyllysine hydrochloride 

Relevant articles and documents

Development of a fluorogenic probe with a transesterification switch for detection of histone deacetylase activity

Histone deacetylases (HDACs) are key enzymatic regulators of many cellular processes such as gene expression, cell cycle, and tumorigenesis. These enzymes are attractive targets for drug development. However, very few simple methods for monitoring HDAC ac

Chemical Synthesis of Cys-Containing Protein via Chemoselective Deprotection with Different Palladium Complexes

We report selective removals of N-terminal and internal Cys protecting groups using different palladium complexes to facilitate the efficient chemical protein synthesis. Utilizing the orthogonal deprotection pairs, we accomplished chemical synthesis of histone H3 containing trimethylated Lys through the combination of Pd(0)-mediated Alloc deprotection for one-pot multiple peptide ligation and Pd(II)Cl2-mediated Acm deprotection to recover native Cys residues after desulfurization.

Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition

Histone lysine methylation is regulated by N?-methyltransferases, demethylases, and N?-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigen

Photoactive spatial proximity probes for binding pairs with epigenetic marks

A new strategy for encoding polypeptide libraries with photolabile tags is developed. The photoassisted assay, based on conditional release of encoding tags only from bound pairs, can differentiate between peptides which have minor differences in a form o