This recombinant human renin receptor (ATP6AP2) comes from E.coli production, with an expression region covering amino acids 17-350—essentially the complete mature protein. It carries an N-terminal 6xHis-SUMO tag that aids in both purification and detection. SDS-PAGE analysis confirms the product reaches greater than 90% purity, which appears to support reliable research outcomes.
The renin receptor, or ATP6AP2, seems to play an important role in the renin-angiotensin system that helps control blood pressure and electrolyte balance. Beyond these pathways, ATP6AP2 is likely involved in cellular processes like proton transport and protein folding. This makes it particularly interesting for cardiovascular and metabolic research.
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.
The human ATP6AP2 protein requires proper integration into a lipid membrane, specific glycosylation patterns, and likely association with other protein partners for its native structure. The bacterial expression system lacks the endoplasmic reticulum machinery for membrane protein folding, glycosylation capabilities, and eukaryotic chaperones. While the SUMO tag may improve solubility, it cannot compensate for the fundamental limitations of producing a multi-pass transmembrane protein in a prokaryotic system. The probability of this recombinant protein achieving a functional, natively folded conformation is extremely low.
1. Antibody Development and Validation
This recombinant ATP6AP2 serves as a suitable immunogen for generating antibodies that recognize linear epitopes of the protein. The extensive sequence coverage (17-350aa) ensures broad epitope availability. This protein is excellent for generating sequence-specific antibodies. These antibodies will be valuable for techniques like Western blotting under denaturing conditions. However, they will likely not efficiently recognize the native, properly folded, and glycosylated ATP6AP2 in its membrane-embedded state in cellular contexts.
2. Biochemical Characterization and Stability Studies
This is the essential first step to characterize the biophysical properties of this specific protein preparation. Techniques like SEC-MALS and circular dichroism can determine its oligomeric state, stability, and secondary structure content. This data is critical for understanding the protein's quality but describes the properties of a misfolded soluble variant, not the native membrane protein.
Final Recommendation & Action Plan
The utility of the E. coli expression system producing a functional version of this complex transmembrane protein renders it inappropriate for any structure-dependent applications. The immediate and only reliable step is Application 2 (Biochemical Characterization) to understand the physical properties of the produced soluble protein. It can be reliably used for Application 1 (Antibody Development against linear epitopes). Interaction studies and ligand binding assays are not recommended as they require the native membrane-integrated structure. For functional studies of ATP6AP2, the only valid path is to study the endogenous protein from mammalian cells or express the full-length protein in a eukaryotic membrane-containing system (e.g., mammalian, insect, or yeast cells) that supports correct folding, glycosylation, and membrane integration.
