Recombinant Human Telomerase protein component 1 (TEP1) is produced using an E. coli expression system and comes with a 6xHis-tag attached to the N-terminus, which makes purification more straightforward. This product contains a partial protein sequence that spans amino acids 2-226. SDS-PAGE analysis confirms the purity exceeds 90%, which appears suitable for various research applications. This protein is strictly for research use—not intended for diagnostic or therapeutic purposes.
TEP1 is part of the telomerase complex, a cellular machinery that seems crucial for maintaining telomeres—those protective caps found at chromosome ends. The protein likely contributes to telomere length regulation and stability, processes that may be vital for cellular aging and replication. Research on cellular longevity and aging-related mechanisms often focuses on this component.
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
This N-terminal fragment of TEP1 (amino acids 2-226) could help researchers investigate protein-protein interactions within the N-terminal region of this telomerase complex component. The 6xHis tag allows for purification and immobilization in pull-down assays, potentially identifying binding partners or confirming suspected interactions. Researchers might use this recombinant fragment in co-immunoprecipitation experiments and surface plasmon resonance studies to characterize how it binds with other telomerase components or regulatory proteins, including binding kinetics and affinities.
2. Antibody Development and Validation
The recombinant TEP1 fragment works as an antigen for creating specific antibodies targeting the N-terminal region of human TEP1. Its high purity (>90%) and well-defined amino acid sequence (2-226) make it potentially suitable for immunization protocols and antibody screening that follows. Scientists can then validate these antibodies using this recombinant protein in ELISA, Western blot, and other immunoassays to check specificity and determine cross-reactivity profiles.
3. Structural and Biochemical Characterization
This partial TEP1 protein may prove useful in structural biology studies aimed at understanding how the N-terminal region folds and organizes its domains. Biophysical techniques like circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation could provide insights into the protein's secondary structure, oligomerization state, and stability. The defined fragment boundaries (2-226aa) allow researchers to focus their analysis on this specific region's biochemical properties.
4. His-Tag Affinity-Based Assays
The N-terminal 6xHis tag opens up possibilities for developing various affinity-based research assays, including nickel-column chromatography for protein complex purification and His-tag specific ELISA formats. Scientists can immobilize the tagged protein on nickel-coated surfaces to screen for potential small molecule ligands or create binding assays with other cellular components. This approach may help control the orientation and presentation of the TEP1 fragment in experimental setups.
