2231747-83-2
Chemical Structure
MAUra-DTB
- CAS No.: 2231747-83-2
- Formula:C25H38N6O5
- Molecular Weight:502.61
InChIKey: NHLRAYKIQZCELW-GHTZIAJQSA-N
SMILES: O=C1N(C2=CC=C(C=C2)OCCCCCCNC(CCCCC[C@H]3NC(N[C@H]3C)=O)=O)C(NN1C)=O
Biological Activity: MAUra-DTB is a 1-methyl-4-arylurazole (MAUra) chemical probe conjugated with desthiobiotin, which preferentially labels tyrosine residues exposed on protein surfaces under photocatalytic or laccase-catalyzed conditions (). The desthiobiotin moiety of MAUra-DTB supports affinity enrichment based on streptavidin or NeutrAvidin. MAUra-DTB enables proteome-wide labeling in cell lysates, and after enrichment of labeled peptides by NeutrAvidin, the labeling sites can be identified via nanoLC-MS/MS. MAUra-DTB can be used for photocatalytic proximity labeling, target protein identification and proteomic studies[1][2][3].
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MAUra-DTB | MAUra-DTB is a 1-methyl-4-arylurazole (MAUra) chemical probe conjugated with desthiobiotin, which preferentially labels tyrosine residues exposed on protein surfaces under photocatalytic or laccase-catalyzed conditions (). The desthiobiotin moiety of MAUra-DTB supports affinity enrichment based on streptavidin or NeutrAvidin. MAUra-DTB enables proteome-wide labeling in cell lysates, and after enrichment of labeled peptides by NeutrAvidin, the labeling sites can be identified via nanoLC-MS/MS. MAUra-DTB can be used for photocatalytic proximity labeling, target protein identification and proteomic studies. | |||||||||||||||||||||
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- [1]. Sato S, et al. 1-Methyl-4-aryl-urazole (MAUra) labels tyrosine in proximity to ruthenium photocatalysts. Chemical communications (Cambridge, England). 2018 Jun 05;54(46):5871-5874. [Content Brief]
- [2]. Nakane K, et al. Switching of Photocatalytic Tyrosine/Histidine Labeling and Application to Photocatalytic Proximity Labeling. International journal of molecular sciences. 2022 Oct 02;23(19):11622. [Content Brief]
- [3]. Nakane K, et al. Laccase-catalyzed tyrosine click reaction with 1-methyl-4-arylurazole: rapid labeling on protein surfaces. Chemical communications (Cambridge, England). 2024 Nov 28;60(96):14208-14211. [Content Brief]
Keywords