Recombinant Saccharomyces cerevisiae Acyl-CoA-binding protein (ACB1) is expressed in yeast and includes an N-terminal 6xHis tag for efficient purification. This full-length protein spans amino acids 1-87 and shows purity greater than 90% as confirmed by SDS-PAGE. Intended for research use only, it appears to be a reliable tool for various biochemical assays, with low endotoxin levels that make it suitable for sensitive applications.
The Acyl-CoA-binding protein (ACB1) from Saccharomyces cerevisiae likely plays a crucial role in intracellular lipid metabolism. It participates in the binding and transport of acyl-CoA esters, supporting key processes in lipid biosynthesis and degradation. Given its fundamental role in lipid homeostasis, ACB1 has become an important focus in research studying metabolic pathways in eukaryotic cells, particularly in yeast models.
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.
Based on the provided information, recombinant Saccharomyces cerevisiae ACB1 is produced in a yeast expression system as a full-length protein (1-87aa) with an N-terminal 6xHis-tag. This represents a homologous expression scenario where the protein is expressed in its native host organism. Yeast expression systems contain the appropriate chaperones and folding machinery needed for proper ACB1 folding, including the capacity for correct disulfide bond formation if required. ACB1 is a relatively small protein (10 kDa) that typically functions as a monomeric acyl-CoA-binding protein, which simplifies proper folding. The 6xHis tag is small and unlikely to significantly interfere with folding. Purity >90% by SDS-PAGE indicates good production quality. In this homologous system, the probability of correct folding and bioactivity is very high. However, without specific validation data (e.g., acyl-CoA binding assays, circular dichroism), folding and bioactivity cannot be conclusively confirmed without verification, though the system is optimal for producing functional protein.
1. Lipid Metabolism Research and Acyl-CoA Binding Studies
This recombinant ACB1 is suitable for acyl-CoA binding studies since it's expressed in its native host system, which should preserve its natural folding and function. The small His-tag is unlikely to interfere with the binding pocket, making kinetic and specificity studies reliable. Binding assays using surface plasmon resonance or other biophysical methods should yield biologically relevant results that accurately reflect ACB1's role in yeast lipid metabolism.
2. Protein-Protein Interaction Studies
The recombinant ACB1 is well-suited for interaction studies as the native folding ensures proper presentation of interaction interfaces. The His-tag facilitates pull-down assays to identify genuine binding partners in yeast metabolic pathways. Since the protein is correctly folded in its native system, results should accurately reflect ACB1's natural protein interaction networks without significant tag-related artifacts.
3. Antibody Development and Validation
This application is suitable as the recombinant protein presents native conformational epitopes due to proper folding in the yeast expression system. Antibodies generated will likely recognize the natural ACB1 protein in various applications. The high purity and authentic folding ensure that antibodies will have optimal specificity for biological studies in yeast systems.
4. Comparative Protein Structure and Function Analysis
The recombinant ACB1 can be used for comparative studies since the native yeast expression system produces a properly folded protein with an authentic structure. Biophysical characterization (circular dichroism, NMR) will yield accurate data on the native protein's conformation, enabling meaningful cross-species comparisons of acyl-CoA-binding protein evolution and function.
Final Recommendation & Action Plan
This recombinant ACB1 expressed in its native yeast host has a high probability of being properly folded and functional, making it suitable for all proposed applications with minimal concerns. The recommended action plan includes: proceeding with applications while including standard controls; for binding studies, validate with known acyl-CoA ligands as positive controls; for structural comparisons, consider removing the His-tag if highest resolution is needed, though it likely has minimal impact; this protein can be used with high confidence for yeast ACB1 research without the need for extensive validation typically required for heterologous expression systems.
