Journal
STAR PROTOCOLS
Volume 3, Issue 2, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.xpro.2022.101316
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Funding
- Swedish Research Council [2019-06106, 20140811]
- Crafoord Foundation [20180916, 2015-01534]
- Magnus Bergvall Foundation [KAW 2015.0131]
- Knut and Alice Wallenberg Foundation [2020.0194, R313-2019-774]
- Lundbeck Foundation [82000]
- Independent Research Fund Denmark [BB/P025927/1]
- NordForsk [R133-A12689]
- UK Biotechnology amp
- Biosciences Research Council [ECF-2021-602]
- Aston University
- Leverhulme Trust
- [2013-05945]
- [4183-00559]
- Swedish Research Council [2019-06106] Funding Source: Swedish Research Council
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This article describes a protocol for characterizing the interaction between a human AQP and a soluble interaction partner using microscale thermophoresis (MST). The protocol provides a high level of control over components and environment, allowing for investigation of AQP protein-protein interactions with low sample consumption and high detergent compatibility.
Aquaporin water channels (AQPs) are membrane proteins that maintain cellular water homeostasis. The interactions between human AQPs and other proteins play crucial roles in AQP regulation by both gating and trafficking. Here, we describe a protocol for characterizing the interaction between a human AQP and a soluble interaction partner using microscale thermophoresis (MST). MST has the advantage of low sample consumption and high detergent compatibility enabling AQP protein-protein interaction investigation with a high level of con-trol of components and environment. For complete details on the use and execution of this protocol, please refer to Kitchen et al. (2020) and Roche et al. (2017).
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