Recombinant Mouse Serum amyloid A-1 protein (Saa1) gets produced in E. coli and includes the full length of the mature protein, spanning amino acids 20 to 122. The protein features an N-terminal 6xHis-tag designed to help with purification and detection. SDS-PAGE analysis shows purity levels above 85%, which appears to make it suitable for various research applications.
Serum amyloid A-1 protein likely plays a significant role in the acute phase response, getting involved in lipid metabolism and immune function regulation. It's a key component in chronic inflammation studies. Researchers often examine it in the context of amyloid fibril formation. This protein seems essential for understanding inflammatory processes and how the body responds to injury or infection.
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. In Vitro Protein-Protein Interaction Studies
This recombinant mouse Saa1 protein can investigate binding interactions with potential cellular receptors, co-factors, or other serum proteins in controlled laboratory environments. The N-terminal 6xHis tag helps with immobilization on nickel-coated surfaces or beads for pull-down assays to identify binding partners. High purity levels (>85%) may ensure reliable results in biochemical binding studies and surface plasmon resonance experiments. Such studies could help clarify the molecular mechanisms underlying Saa1 function in acute phase responses.
2. Antibody Development and Validation
The purified recombinant Saa1 protein works as an antigen for generating mouse Saa1-specific antibodies in research settings. Researchers can use the protein to immunize rabbits or other suitable host animals to produce polyclonal antibodies. It also serves as a screening antigen for monoclonal antibody development. The 6xHis tag allows for easy purification and immobilization in ELISA-based antibody screening and characterization assays. These antibodies would likely prove valuable as research tools for studying Saa1 expression and localization in mouse models of inflammation and disease.
3. Structural and Biophysical Characterization
This recombinant protein provides material for investigating the structural properties of mouse Saa1 through various biophysical techniques. These include circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation. The mature protein region (20-122aa) represents the biologically relevant form, making it suitable for studying protein folding, stability, and aggregation properties. High purity levels support reliable structural analysis and comparison with other serum amyloid A family members across different species.
4. In Vitro Functional Assays
Researchers can use the recombinant Saa1 protein in cell culture-based assays to study its effects on various cell types relevant to inflammatory responses. This protein allows investigation of cellular uptake mechanisms, cytokine induction, or cell signaling pathway activation in macrophages, hepatocytes, or other relevant cell lines. The defined concentration and purity of the recombinant protein enables dose-response studies and mechanistic investigations of Saa1 function under controlled experimental conditions.
5. Comparative Species Analysis
This mouse-specific Saa1 protein makes possible comparative studies with human or other mammalian serum amyloid A proteins to understand species-specific differences in structure and function. Researchers can use the recombinant protein alongside human SAA1 in parallel biochemical assays to identify conserved versus divergent properties. Such comparative analyses may contribute to understanding the evolutionary conservation of serum amyloid A function. They might also inform the selection of appropriate animal models for research studies.
