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Updated: May 2, 2026

Identification of Protein Interacting Partners Using Tandem Affinity Purification
Published on: February 25, 2012
[Identification of proteins interacted with Bat3 using tandem affinity purification].
Wei Wu1, Qin-shan Li1, Wei Song1
1National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005, China.
This study identified Ubiquitin-like protein 4A (Ubl4A) as a key binding partner of Bat3, revealing its role in Bat3-mediated apoptosis. Tandem affinity purification confirmed this crucial protein interaction.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Context:
- The protein Bat3 (also known as BAG6) plays a critical role in cellular processes, including apoptosis.
- Understanding Bat3's molecular interactions is essential for elucidating its function in cell death pathways.
Purpose:
- To identify novel protein interactors of Bat3 involved in apoptosis.
- To validate the interaction between Bat3 and its binding partners using biochemical methods.
Summary:
- Tandem affinity purification (TAP) was employed to screen for Bat3-interacting proteins using full-length human Bat3 as bait.
- Mass spectrometry identified Ubiquitin-like protein 4A (Ubl4A) as a Bat3-binding partner.
- Co-immunoprecipitation assays confirmed the physical association between Bat3 and Ubl4A.
Impact:
- This research establishes TAP as a viable method for identifying Bat3 binding partners.
- The identification of Ubl4A as a Bat3 interactor provides new insights into the mechanisms of Bat3-mediated apoptosis.
- These findings open avenues for further investigation into the therapeutic potential of targeting the Bat3-Ubl4A interaction in apoptotic pathways.
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