One benefit of such an approach is that cellular regions that cannot be purified, such as synaptic clefts, can nevertheless be studied by proteomic mapping. Furthermore, since targeted tagging is performed on whole cells, cellular components that would usually be destroyed by cell lysis and purification (e.g. protein complexes or membranes) are left intact while the biotinylation reaction occurs, and the probability of generating artifacts is greatly reduced.

Principle of proximity labeling of cell-surface proteins with Biotin-AEEA-Tyramide.

Our hydrophilic Biotin-AEEA-Tyramide (LS-3490), which bears a short PEG spacer between the biotin and the phenol moieties, is a membrane-impermeant variant of regular Biotin-Tyramide (LS-3500). Biotin-AEEA-Tyramide can thus be used for the selective biotinylation of cell surface proteins. It has been shown to be membrane-impermeant when used for a short time on cultured cells (ca. 1 min during the biotinylation reaction).

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References:

• Mapping the Proteome of the Synaptic Cleft through Proximity Labeling Reveals New Cleft Proteins; T. Cijsouw, A. Ramsey, T. Lam, B. Carbone, T. Blanpied and T. Biederer; 2018; 6: 48.