The Recombinant Human Heat shock 70 kDa protein 6 (HSPA6) is expressed in E. coli and features a partial sequence from the 1-637 amino acid region. This protein comes with an N-terminal 6xHis-tag, which makes purification and detection more straightforward in research applications. It reaches a purity greater than 90%, as verified by SDS-PAGE, which appears to ensure high-quality results for experimental use. This product is intended for research purposes only.
HSPA6 belongs to the heat shock protein 70 family, which may play a crucial role in cellular stress response mechanisms. It acts as a molecular chaperone, helping with the proper folding of nascent and stress-accumulated proteins while preventing protein aggregation. The study of HSPA6 seems important for understanding cellular homeostasis and stress response pathways. This makes it a potentially valuable tool in research focused on protein folding and stress conditions.
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. Heat Shock Response Mechanism Studies
This recombinant HSPA6 protein can be used to investigate the molecular mechanisms of cellular heat shock responses in vitro. Researchers might study protein-protein interactions between HSPA6 and other heat shock proteins or co-chaperones through biochemical assays. The N-terminal 6xHis tag makes purification and immobilization easier for interaction studies. This application could help clarify the specific role of HSPA6 in cellular stress responses compared to other HSP70 family members.
2. Antibody Development and Validation
The purified recombinant HSPA6 protein appears to work well as an antigen for generating specific antibodies against human HSPA6. The high purity (>90%) likely reduces cross-reactivity during immunization protocols. Researchers can use this protein to validate antibody specificity through ELISA, Western blot, and other immunoassays. The His-tag allows for easy immobilization on nickel-coated surfaces for antibody screening and characterization.
3. Protein Folding and Chaperone Activity Assays
This recombinant HSPA6 can be used in in vitro protein folding assays to study its potential chaperone functions. Researchers might investigate whether HSPA6 assists in refolding of denatured substrate proteins under controlled laboratory conditions. The purified protein allows for systematic studies of cofactor requirements and optimal conditions for any chaperone activity. Such studies would contribute to understanding the biochemical properties of this specific HSP70 family member.
4. Structural and Biophysical Characterization
The recombinant HSPA6 protein provides material for detailed structural studies using techniques such as X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy. Researchers can analyze the protein's conformational states and domain organization. The high purity level makes it suitable for biophysical analyses including thermal stability studies, circular dichroism spectroscopy, and dynamic light scattering experiments. These studies would likely provide insights into the structural basis of HSPA6 function.
5. Pull-down Assays for Interaction Partner Identification
The N-terminal His-tag enables efficient pull-down experiments to identify cellular proteins that interact with HSPA6. Researchers can immobilize the recombinant protein on nickel-affinity matrices and incubate with cell lysates or purified protein libraries. This approach allows for systematic identification of potential binding partners and regulatory proteins. The high purity of the recombinant protein appears to minimize background interactions and improve the reliability of interaction studies.
