Recombinant Human Transcriptional enhancer factor TEF-3 (TEAD4) is produced in an E.coli expression system, covering the amino acid region 74-434. This partial-length protein features an N-terminal 6xHis-SUMO tag, which helps with purification and detection. The product shows a purity level greater than 90%, confirmed by SDS-PAGE analysis. It's designed for research use only and is not intended for diagnostic or therapeutic applications.
TEAD4, also known as Transcriptional enhancer factor TEF-3, appears to play a crucial role in gene expression regulation by binding to specific DNA sequences. It serves as a key component in the Hippo signaling pathway, which controls cell growth and apoptosis. TEAD4 seems instrumental in developmental processes and cellular proliferation studies, making it a significant focus in various research areas.
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-DNA Interaction Studies
This recombinant TEAD4 fragment (74-434aa) contains the DNA-binding domain and can be used in electrophoretic mobility shift assays (EMSA) to study its binding affinity to TEAD-responsive elements. The N-terminal 6xHis-SUMO tag helps with protein purification and detection without interfering with the DNA-binding region. Researchers might investigate the specificity of TEAD4-DNA interactions by testing various DNA sequences and measuring binding kinetics. The >90% purity makes this protein suitable for quantitative binding studies and competition assays.
2. Antibody Development and Validation
The recombinant TEAD4 protein can serve as an antigen for generating specific antibodies against human TEAD4. The 6xHis tag allows easy immobilization on nickel-coated surfaces for ELISA-based antibody screening and characterization. This protein fragment covers a substantial portion of TEAD4 and can be used to validate antibody specificity in Western blot and immunoprecipitation experiments. The E. coli expression system appears to offer cost-effective production of antigen for large-scale antibody development projects.
3. Protein-Protein Interaction Mapping
The TEAD4 fragment may be useful in pull-down assays to identify and characterize protein partners that interact with the central region of TEAD4. The 6xHis tag allows for immobilization on nickel-affinity resins, which enables capture of interacting proteins from cell lysates or purified protein libraries. This application is particularly valuable for studying YAP/TAZ-TEAD4 interactions and other cofactor binding events. The high purity of the protein likely reduces background binding and improves the reliability of interaction studies.
4. Biochemical Characterization Studies
This recombinant protein can be used for detailed biochemical analysis including thermal stability studies, pH sensitivity assays, and buffer optimization experiments. The defined protein boundaries (74-434aa) make it suitable for domain-specific functional studies and structure-activity relationship investigations. Researchers can perform comparative studies with other TEAD family members using this standardized protein preparation. The consistent purity and expression system may enable reproducible biochemical characterization across different laboratories.
