Proximity Labeling Proteomics

Proximity labeling proteomics is an advanced biochemical approach designed to map protein spatial relationships and dynamic interactions within cells. By genetically fusing specific enzymes such as biotin ligase BirA or peroxidase APEX to target proteins, these enzymes can selectively label proximal proteins with biotin tags. The biotinylated proteins are subsequently enriched via streptavidin affinity purification and analyzed using high-resolution mass spectrometry for identification and quantification.

 

This technology excels in studying intracellular protein networks, signal transduction pathways, and spatial protein localization. Unlike traditional proteomics techniques that often rely on cell lysis and extensive protein fractionation, which may disrupt transient or weak protein interactions, proximity labeling proteomics allows in situ protein tagging in live cells. This preserves the native cellular environment and provides spatially resolved proteomic insights. Such advantages are particularly crucial in examining dynamic cellular events, including cell division, polarity establishment, and signal transduction pathways. For instance, in neuroscience, proximity labeling proteomics enables the differentiation of pre- and postsynaptic proteomes, offering valuable insights into synaptic signal transmission mechanisms.

 

The applications of proximity labeling proteomics extend across diverse fields, including cell biology, neuroscience, oncology, and infectious disease research. In organelle interaction studies, it facilitates the identification of protein complexes localized at specific subcellular interfaces, such as the endoplasmic reticulum-mitochondria junction. Additionally, by tagging transcription factors with APEX peroxidase, researchers can characterize interacting proteins and associated molecular partners, shedding light on gene regulatory networks.

 

A significant strength of proximity labeling proteomics lies in its ability to detect low-abundance proteins and capture transient interactions. Many protein interactions occur briefly and under specific cellular conditions, making them challenging to detect with traditional co-immunoprecipitation methods. In contrast, proximity labeling proteomics enables rapid and specific protein tagging, preserving transient protein interactions and improving spatiotemporal resolution. This capability holds immense potential in signal transduction analysis and drug target discovery.

 

At MtoZ Biolabs, we offer end-to-end proximity labeling proteomics services, encompassing experimental design, sample preparation, affinity purification, and mass spectrometry data analysis. Our team of experts ensures precision, reproducibility, and tailored support to help researchers uncover protein interaction networks in dynamic cellular contexts, advancing biological discovery and therapeutic innovation.

 

MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.