23500-04-1

Basic information

• Product Name: AC-LYS (BOC)-OH
• Synonyms: AC-LYSINE (BOC)-OH;AC-LYS (BOC)-OH;ACETYL-N-EPSILON-BOC-L-LYSINE;N-ALPHA-ACETYL,N-EPSILON-T-BUTOXYCARBONYL-L-LYSINE;N2-Acetyl-N6-(tert-butoxycarbonyl)-L-lysine;(S)-2-AcetaMido-6-((tert-butoxycarbonyl)aMino)hexanoic acid;N2-Acetyl-N6-[(1,1-dimethylethoxy)carbonyl]-L-lysine;Ac-Lys(Boc)
• CAS NO: 23500-04-1
• Molecular Formula: C₁₃H₂₄N₂O₅
• Molecular Weight: 288.34
• Mol File: 23500-04-1.mol

Chemical Properties

• Melting Point: 128 °C
• Boiling Point: 528.8±45.0 °C(Predicted)
• Appearance: White/Powder
• Density: 1.124±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 3.65±0.10(Predicted)
• CAS DataBase Reference: AC-LYS (BOC)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: AC-LYS (BOC)-OH(23500-04-1)
• EPA Substance Registry System: AC-LYS (BOC)-OH(23500-04-1)

Safety Data

• Hazardous Substances Data: 23500-04-1(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

• 2418-95-3 (S)-2-amino-6-(tert-butoxycarbonylamino)hexanoic acid 
• 108-24-7 acetic anhydride 
• 24424-99-5 di-tert-butyl dicarbonate 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 1946-82-3 N-Ac-L-Lys-OH 
• 75-36-5 acetyl chloride 
• 657-27-2 L-Lysine hydrochloride 

Downstream Products

• 156661-42-6 Ac-Lys-AMC 
• 148101-51-3 N²-acetyl-N⁶-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-lysine 
• 1609108-48-6 N²-acetyl-N⁶-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-lysyl-L-valyl-N⁵-carbamoyl-N-[4-(hydroxymethyl)phenyl]-L-ornithinamide 
• 1609108-49-7 N²-acetyl-N⁶-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-lysyl-L-valyl-N⁵-carbamoyl-N-[4-({[(4-nitrophenoxy)carbonyl]oxy}methyl)phenyl]-L-ornithinamide 
• 1610892-91-5 [5-acetylamino-5-[2-(4-sulfamoylphenyl)ethylcarbamoyl]pentyl]carbamic acid tert-butyl ester 
• 1610892-89-1 [5-acetylamino-5-(4-sulfamoylbenzylcarbamoyl)pentyl]carbamic acid tert-butyl ester 
• 1946-82-3 N-Ac-L-Lys-OH 

Relevant articles and documents

Intramolecular long-distance nucleophilic reactions as a rapid fluorogenic switch applicable to the detection of enzymatic activity

Long-distance intramolecular nucleophilic reactions are promising strategies for the design of fluorogenic probes to detect enzymatic activity involved in lysine modifications. However, such reactions have been challenging and hence have not been established. In this study, we have prepared fluorogenic peptides that induce intramolecular reactions between lysine nucleophiles and electrophiles in distal positions. These peptides contain a lysine and fluor-escence-quenched fluorophore with a carbonate ester, which triggers nucleophilic transesterification resulting in fluorogenic response. Transesterification occurred under mild aqueous conditions despite the presence of a long nine-amino-acid spacer between the lysine and fluorophore. In addition, one of the peptides showed the fastest reaction kinetics with a half-life time of 3.7 min. Furthermore, the incorporation of this fluorogenic switch into the probes allowed rapid fluorogenic detection of histone deacetylase (HDAC) activity. These results indicate that the transesterification reaction has great potential for use as a general fluorogenic switch to monitor the activity of lysine-targeting enzymes.

18F-Trifluoromethylation of Unmodified Peptides with 5-18F-(Trifluoromethyl)dibenzothiophenium Trifluoromethanesulfonate

The 18F-labeling of 5-(trifluoromethyl)-dibenzothiophenium trifluoromethanesulfonate, commonly referred to as the Umemoto reagent, has been accomplished applying a halogen exchange 18F-fluorination with 18F-fluoride, follo

Sulfonamides with potent inhibitory action and selectivity against the α-carbonic anhydrase from Vibrio cholerae

By using N-α-acetyl-l-lysine or GABA scaffolds and the conversion of the terminal amino group to the guanidine one, benzenesulfonamides incorporating water solubilizing moieties were synthesized. The new compounds were medium potency inhibitors of the cyt

SPLICEOSTATIN ANALOGS

The present invention is directed to novel cytotoxic spliceostatin analogs (I) and derivatives, to antibody drug conjugates thereof, and to methods for using the same to treat medical conditions including cancer.

A magnetic biomimetic nanocatalyst for cleaving phosphoester and carboxylic ester bonds under mild conditions

As a result of the unique surface structure of nanospheres, Asp and His residues supported on a 12 nm maghemite nanoparticle worked collaboratively as a biomimetic nanocatalyst for hydrolyzing paraoxon (phosphoester) and 4-nitrophenyl acetate (carboxylic ester) in Milli-Q water (pH 7.0) at 37 °C, without employing extremes of pH or heavy metals. Our nanocatalyst could be facilely recovered via magnetic concentration. The isolated catalyst exhibited long-term stability, showing no significant loss of its catalytic activity for repeated uses after 3 months.

Reactivity of Lysine Moieties toward γ-Hydroxy-α,β-unsaturated Epoxides: A Model Study on Protein-Lipid Oxidation Product Interaction

Epoxyols are generally accepted as crucial intermediates in lipid oxidation. The reactivity of γ-hydroxy-α,β-unsaturated epoxides toward lysine moieties is investigated, employing trans-4,5-epoxytrans-2-hexen-1-ol (EH) as a model substrate and propylamine or N2-acetyl-L-lysine 4-methylcoumar-7-ylamide (AcLys-MCA) as model reagents for protein-bound lysine. Independent syntheses are reported for EH and AcLys-MCA. Reaction of the amine components with EH in THF yields 4-(propylamino)-trans-2-hexene-1,5-diol and N2-acetyl-N6-(1,5-dihydroxy-trans-2-hexen-4-yl)-L-lysine 4-methylcoumaryl-7-amide, respectively. Unequivocal structural characterization of the products prove the epoxy ring cleavage to proceed by a true SN2 mechanism. Incubation of EH with propylamine and AcLys-MCA in aqueous medium at 37 °C shows the turnover to decrease with lower pHs. From reaction of EH (100 mM) with AcLys-MCA (50 mM) under physiological conditions (pH 7.4), 3% of the lysine moieties can be identified in the form of N2-acetyl-N6-(1,5-dihydroxy-trans-2-hexen-4-yl)-L-lysine 4-methylcoumar-7-ylamide after 24 h.