Recombinant Human Estrogen receptor beta (ESR2) comes from yeast expression and includes an N-terminal 6xHis-tag that makes purification and detection much simpler. The protein covers amino acids 2 to 530, which represents a partial but substantial portion of the complete sequence. Purity levels exceed 90% based on SDS-PAGE analysis, though this should provide reliable performance in most downstream work.
Estrogen receptor beta (ERβ) belongs to the nuclear receptor family of intracellular receptors. This protein appears to play an essential role in how estrogens work throughout the body, affecting both gene expression and how cells function. ERβ seems to be involved in reproductive health, cardiovascular processes, and bone maintenance - areas that make it particularly interesting for researchers studying hormone signaling networks.
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.
1. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
The N-terminal 6xHis-tag makes this recombinant ESR2 protein well-suited for nickel-affinity pull-down experiments when hunting for binding partners. Since the expressed region (2-530aa) covers most of the receptor, it likely includes the important interaction domains researchers need. The approach is straightforward: immobilize the His-tagged ESR2 on nickel beads, then incubate with cell lysates or purified proteins to fish out whatever binds. With purity above 90%, background contamination during these interaction studies may be less of a concern.
2. Antibody Development and Validation
This purified recombinant ESR2 protein could work well as an antigen for creating antibodies specific to human estrogen receptor beta. The combination of high purity and substantial protein length makes it a reasonable choice for animal immunization or screening antibody libraries that already exist. The His-tag also simplifies purification and immobilization in ELISA screening assays, which helps when identifying and confirming antibody specificity. Both monoclonal and polyclonal antibody development appears feasible with this material.
3. Biochemical Characterization and Stability Studies
Detailed biochemical analysis becomes possible with this recombinant ESR2 protein - things like thermal stability, pH sensitivity, and finding optimal buffer conditions. Dynamic light scattering, differential scanning fluorimetry, or analytical ultracentrifugation might reveal useful information about the protein's biophysical behavior. The yeast expression background and high purity suggest this protein could handle systematic studies examining how various conditions influence stability and whether aggregation becomes problematic.
4. Competitive Binding Assays and Ligand Screening
Even though biological activity hasn't been tested, this recombinant ESR2 protein may still prove useful in competitive binding assays for screening potential ligands or inhibitors. The His-tag allows straightforward immobilization on nickel-coated plates or beads during binding studies. Fluorescence polarization or surface plasmon resonance assays could measure how known ligands bind and help screen compound libraries for new receptor interactions, though results would need careful interpretation given the unknown activity status.
