Recombinant Human Heat shock protein HSP 90-alpha (HSP90AA1) is produced in E. coli and contains amino acids 292 to 559, which represents a partial sequence of the protein. The protein carries an N-terminal 6xHis-tag that helps with purification and detection. The purity level exceeds 85% as verified by SDS-PAGE. This product is designed for research use only, though it appears to deliver reliable performance in laboratory settings.
HSP90AA1, commonly called Heat shock protein HSP 90-alpha, is a chaperone protein that may play a critical role in stabilizing and folding other proteins, particularly when cells face stress. It seems to be involved in various cellular processes, including protein maturation and degradation pathways. HSP90 has become a focal point in research because it's likely involved in maintaining cellular homeostasis, and there are potential implications in disease-related protein misfolding.
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. HSP90 C-terminal Domain Structural Studies
This recombinant protein fragment (292-559aa) represents the C-terminal domain of HSP90AA1. This region appears to be critical for client protein binding and co-chaperone interactions. Researchers can use the purified protein in X-ray crystallography or NMR studies to investigate structural features of this domain in isolation. The N-terminal 6xHis tag makes purification and immobilization easier for structural biology applications. Studies like these could provide insights into the molecular mechanisms of HSP90's chaperone function at the C-terminal region.
2. Antibody Development and Validation
The recombinant HSP90AA1 C-terminal domain can serve as an immunogen or screening antigen for developing domain-specific antibodies. The defined amino acid sequence (292-559aa) allows scientists to generate antibodies that specifically recognize the C-terminal region of HSP90AA1. The 6xHis tag makes purification and immobilization straightforward in ELISA-based screening assays during antibody development. These antibodies could become valuable research tools for studying HSP90AA1 localization and expression patterns.
3. Protein-Protein Interaction Studies
The C-terminal domain of HSP90AA1 is known to interact with various co-chaperones and client proteins. This makes the recombinant fragment suitable for in vitro binding studies. The 6xHis tag allows for immobilization on nickel-based surfaces or beads for pull-down assays to identify and characterize binding partners. Researchers can use this protein in surface plasmon resonance or other biophysical techniques to measure binding kinetics and affinities. Such studies would help clarify the specific role of the C-terminal domain in HSP90's chaperone network.
4. Biochemical Characterization of Domain Function
This isolated C-terminal domain can be used to study the intrinsic properties and stability of this specific region of HSP90AA1. Researchers can perform thermal stability assays, circular dichroism spectroscopy, and other biophysical analyses to characterize the folding and stability properties of this domain. The recombinant protein allows investigation of how the C-terminal domain behaves independently of the full-length protein. These studies could provide fundamental insights into the contribution of this domain to overall HSP90 function and stability.
