Recombinant Human Aquaporin-1 (AQP1) is produced in E.coli, covering amino acid region 220-269 with an N-terminal GST tag that helps with solubility and purification. The protein comes with purity levels exceeding 90%, confirmed through SDS-PAGE analysis, which should provide reliable results for experimental work. This product is meant for research use only and isn't intended for therapeutic or diagnostic purposes.
Aquaporin-1 (AQP1) is a water channel protein that moves water across cell membranes, playing an important role in various physiological processes. The protein is involved in regulating water homeostasis and appears to be a key component in several tissues, including the kidney, lung, and vascular system. AQP1's function in water transport makes it a valuable target for research on fluid balance and cellular hydration.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
AQP1 is a transmembrane channel protein whose function depends on its complete six-transmembrane helix structure forming a proper pore. This partial fragment (50 amino acids) represents only a small intracellular portion of the protein and lacks the transmembrane domains necessary for native folding. The GST tag may further interfere with proper structural formation. While the protein may be soluble, it is highly unlikely to adopt any biologically relevant conformation or possess water channel activity. The probability of correct folding is extremely low. Using a misfolded, isolated domain of a membrane protein for interaction screening is highly likely to generate misleading results.
1. Antibody Development and Validation
This AQP1 fragment serves as a suitable immunogen for generating antibodies specific to this C-terminal region. The high purity minimizes antibodies against contaminants. These antibodies will be particularly useful for detecting linear epitopes in techniques like Western blotting. However, they may not recognize conformational epitopes present on the full-length, membrane-embedded protein.
2. Biochemical Characterization of Protein Stability
This application is the essential first step to characterize the biophysical properties of this fragment. Techniques like circular dichroism can assess if it has any defined secondary structure (e.g., alpha-helical content, as this region is intracellular and may be structured) and determine its stability under various conditions. This data is crucial for understanding the behavior of this isolated domain.
Final Recommendation & Action Plan
This recombinant AQP1 protein is a fragment of a complex membrane protein and is unlikely to be correctly folded, limiting its applications to non-structural uses. The immediate priority is Application 2 (Biochemical Characterization) to determine if the fragment has any inherent structure and to establish its stability profile. It is reliable for Application 1 (Antibody Development). Interaction studies and binding assays must be avoided as they require a native fold. For functional studies of AQP1 interactions, the recommended path is to use the full-length protein reconstituted in liposomes or to study interactions in a cellular context where the protein is properly localized and folded. This AQP1 protein should be considered primarily as an antigen source, not a functional protein domain.
