Cy3 hydrazide bromide is a fluorescent probe for carbonylated proteins. Cy3 hydrazide bromide covalently links to aldehyde or ketone residues on carbonylated proteins, reacts with protein carbonyl groups to form stable hydrazones, and enables fluorescent detection (Ex/Em = 555/570 nm) [1] [2] [3].
In Vitro, Cy3 hydrazide bromide (30 min (on ice labeling)) labels carbonylated proteins in mouse latissimus dorsi muscle extracts[1]. Cy3 hydrazide bromide (5 mM; 30 min) enables multiplexed detection of carbonylated proteins in hydrogen peroxide-treated Saccharomyces cerevisiae W303-1A cell extracts via two-dimensional gel electrophoresis, but with spot shifting that reduces alignment with total protein stain[2]. Cy3 hydrazide bromide (0.5-40 mM; 45 min-2 h) labels yeast tRNAPhe at dihydrouridine residues[3]. Cy3 hydrazide bromide (40 mM; 2 h) labels reduced Escherichia coli tRNAArg[3].
References:
[1]. Nina-Diogo A, et al. Synthesis of New Bodipy Hydrazide Fluorescent Probes for the Detection of Carbonylated Proteins Generated by Oxidative Stress. Chembiochem. 2024;25(19):e202400093.
[2]. Tamarit J, et al. Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides. J Proteomics. 2012;75(12):3778-3788.
[3]. Pan D, et al. Synthesis and functional activity of tRNAs labeled with fluorescent hydrazides in the D-loop. RNA. 2009;15(2):346-354.
In Vitro, Cy3 hydrazide bromide (30 min (on ice labeling)) labels carbonylated proteins in mouse latissimus dorsi muscle extracts[1]. Cy3 hydrazide bromide (5 mM; 30 min) enables multiplexed detection of carbonylated proteins in hydrogen peroxide-treated Saccharomyces cerevisiae W303-1A cell extracts via two-dimensional gel electrophoresis, but with spot shifting that reduces alignment with total protein stain[2]. Cy3 hydrazide bromide (0.5-40 mM; 45 min-2 h) labels yeast tRNAPhe at dihydrouridine residues[3]. Cy3 hydrazide bromide (40 mM; 2 h) labels reduced Escherichia coli tRNAArg[3].
References:
[1]. Nina-Diogo A, et al. Synthesis of New Bodipy Hydrazide Fluorescent Probes for the Detection of Carbonylated Proteins Generated by Oxidative Stress. Chembiochem. 2024;25(19):e202400093.
[2]. Tamarit J, et al. Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides. J Proteomics. 2012;75(12):3778-3788.
[3]. Pan D, et al. Synthesis and functional activity of tRNAs labeled with fluorescent hydrazides in the D-loop. RNA. 2009;15(2):346-354.
















