Snap-tagged Receptors

SNAP-tagged receptors are genetically engineered cell-surface receptors fused to a SNAP-tag, a self-labeling protein domain that enables selective labeling and analysis in living cells. The tag reacts covalently with synthetic benzylguanine derivatives, allowing researchers to attach fluorescent dyes, biotin, or other functional probes without disrupting the receptor’s encoded structure. In bioengineering, this system supports real-time visualization of receptor expression, trafficking, internalization, and recycling, while enabling controlled surface labeling and multiplexed imaging. These capabilities help researchers study cell signaling, engineer responsive cells, and evaluate receptor-based therapies with greater spatial and temporal precision.

Snap-tagged Receptors - Related Videos

Research

JoVE Journal - Biology
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Fluorescent Labeling of COS-7 Expressing SNAP-tag Fusion Proteins for Live Cell Imaging

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Cited by 8 •

2010

SNAP-tag and CLIP-tag protein labeling systems enable the specific, covalent attachment of molecules, including fluorescent dyes, to a protein of interest in live cells. Once cloned and expressed, the tagged protein can be used with a variety of substrates for numerous downstream applications without having to clone again.

Education

JoVE Science Education - Psychology

Evaluating the Accuracy of Snap Judgments

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2023

Source: Diego Reinero & Jay Van Bavel—New York University Social psychologists have long been interested in the way people form impressions of others. Much of this work has focused on the errors people make in judging others, such as the exaggerated influence of central traits (such as "warm" and "cold"), the insufficient weight given to the context in which others' behavior takes place, and the tendency for people to make judgments that conform to their initial expectations about another.

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

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Cited by 2 •

2017

A construct encoding TMEM184A with a GFP tag at the carboxy-terminus designed for eukaryotic expression, was employed in assays designed to confirm the identification of TMEM184A as a heparin receptor in vascular cells.

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking

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Cited by 5 •

2014

Here we demonstrate the use of fluorescent Alexa dye coupled to α-bungarotoxin to measure GABA A receptor surface localization and endocytosis in hippocampal neurons. Through the use of constructs bearing a short extracellular tag that binds α-bungarotoxin, analysis of plasma membrane protein endocytic trafficking can be achieved.

Utilizing pHluorin-tagged Receptors to Monitor Subcellular Localization and Trafficking

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Cited by 3 •

2017

Labeling the extracellular domain of a membrane protein with a pH sensitive fluorophore, superecliptic pHluorin (SEP), allows subcellular localization, expression, and trafficking to be determined. Imaging SEP-labeled proteins with total internal reflection fluorescence microscopy (TIRFM) enables the quantification of protein levels in the peripheral ER and plasma membrane.

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