Introduction of CAS:55260-24-7 | N-Boc-N'-(9-xanthenyl)-L-glutamine
Boc-Gln(Xan)-OH, also known as Boc-Gln-Ala-Arg-AMC , is primarily a fluorogenic substrate for the enzyme trypsin . Trypsin is a serine protease that plays a crucial role in protein digestion and other biological processes .
Specification of CAS:55260-24-7 | N-Boc-N'-(9-xanthenyl)-L-glutamine
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ITEMS |
SPECIFICATION |
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Form |
Powder |
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Purity |
97% |
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Boiling point |
669.8±55.0 °C(Predicted) |
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Storage condition |
Sealed in dry,Room Temperature |
Research Application of CAS:55260-24-7 | N-Boc-N'-(9-xanthenyl)-L-glutamine
Hydrolysis of Primary Amide Groups in Peptides : Boc-Gln(Xan)-OH and related peptides can undergo hydrolysis under specific conditions, transforming into different peptide structures. This process is relevant in understanding peptide behavior and reactions in bioorganic chemistry (Onoprienko, Yelin, & Miroshnikov, 2000).
Facile Synthesis of Protected Amino Acids : Boc-Gln(Xan)-OH plays a role in the synthesis of protected amino acids, specifically in the synthesis of Nalpha-Boc-L-alpha,gamma-diaminobutyric acid. This is crucial for developing specific peptides for medical and biochemical applications (Yamada, Urakawa, Oku, & Katakai, 2004).
Photocatalytic Nitrogen Fixation : The Boc-abbreviation (e.g., BOC in Bismuth Subcarbonate, Bi2O2CO3) is used in the synthesis of materials with photocatalytic properties, useful in nitrogen fixation and other environmental applications. This reflects the broader scope of research involving related compounds (Xu et al., 2018).
Enantiomer Separation in NMR Spectroscopy : BOC-Gln(Xan)-OH has been identified as a chiral shift reagent effective in separating the enantiomers of V-agents in 31P-NMR spectroscopy. This application is significant in analytical chemistry for studying chiral compounds (Koller, Thiermann, & Worek, 2019).
Synthesis of HIV Proteinase Substrate Analogs : In the study of HIV proteinase, Boc-Gln(Xan)-OH and its derivatives are used for synthesizing analogs of HIV proteinase substrates, contributing to the understanding of HIV proteinase behavior and potential treatments (Bláha, Nemec, Tözsér, & Oroszlan, 1991).
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