STEAP2 is a vital membrane protein predominantly found in prostate cells, where it plays a key role in metal ion reduction and transport. Its involvement in essential cellular processes, particularly in tumor proliferation, makes STEAP2 a significant target for cancer therapy research. Understanding and manipulating STEAP2 can offer new avenues for therapeutic development, making it an invaluable protein for researchers focusing on cancer and related fields. Leveraging over a decade of expertise in membrane proteins, we have successfully developed and characterized a full-length recombinant STEAP2 protein that meets the high standards required for advanced research, including structural-based drug discovery.
At Eurofins CALIXAR, we understand the challenges of producing membrane proteins in their native, functional states—a critical factor in ensuring the accuracy and reliability of your research. Traditional approaches to membrane protein production frequently face limitations, such as producing proteins that are either locked in a single conformation or significantly altered through truncation and mutation. These methods can compromise the protein’s functional integrity, resulting in samples that are impure, non-native, and less effective for research purposes. Unlike conventional methods that often result in truncated, mutated, or unstable proteins, our proprietary technology and expertise ensure the preservation of STEAP2’s full-length, wild-type structure, complete with its native post-translational modifications.
Eurofins CALIXAR overcomes these challenges by maintaining the native state of the STEAP2 protein throughout the entire production process. Our STEAP2 protein is characterized by exceptional purity, achieving a 90% purity level as confirmed by SDS-PAGE analysis. Beyond purity, the protein is cryostable, maintaining its structural integrity at 4°C for 72h and through up to three freeze-thaw cycles. Additionally, our STEAP2 protein is fully active, demonstrated by its ability to bind heme effectively, with clear functional validation via UV spectroscopy (fig. 1). These attributes—purity, activity, stability, and functionality—highlight Eurofins CALIXAR's commitment to providing high-quality proteins that meet the stringent demands of advanced research.
Our highly pure, active, and stable STEAP2 protein that accurately represents its natural state, making it an ideal candidate for structural-based drug discovery (SBDD) and other advanced research applications. In collaboration with our partner Eyen, we have successfully validated the protein's suitability for Cryo-Electron Microscopy (CryoEM), a crucial technique for high-resolution structural analysis. The STEAP2 protein demonstrated its capacity to reach very high resolution (~2.1Å), with all key ligands, including FAD, NADPH, HEME, and lipids, clearly resolved in the CryoEM structure (fig.2). These detailed structural insights enable precise ligand modeling and protein-ligand interaction analysis, making our STEAP2 protein a powerful tool for accelerating the discovery and development of novel cancer therapies.
Take your structure-based drug design discovery efforts to the next level with our STEAP2 protein!
