Recombinant Macrococcus caseolyticus Oleate hydratase (MCCL_0076) is produced in E. coli and includes an N-terminal 6xHis-tag that makes purification more straightforward. This protein spans amino acids 1-367 and comes as a partial form with purity above 85% based on SDS-PAGE analysis. The product is strictly for research purposes and should not be used in clinical or diagnostic settings.
Oleate hydratase from Macrococcus caseolyticus appears to play an important role in fatty acid metabolism, converting oleic acid into hydroxy fatty acids. Scientists have shown considerable interest in these enzymes, particularly for studying metabolic pathways that involve lipid modification and breakdown. Research into this hydratase's function and activity may help advance our understanding of microbial biochemistry and could potentially benefit industrial processes that transform fatty acids.
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. Biochemical Characterization of Bacterial Oleate Hydratase Activity
Scientists can use this recombinant protein to explore the enzymatic properties and substrate specificity of oleate hydratase from Macrococcus caseolyticus under controlled laboratory conditions. Enzyme kinetics studies with oleic acid and related unsaturated fatty acids as substrates might help determine key catalytic parameters like Km and Vmax. The N-terminal 6xHis tag makes protein purification simpler and allows for immobilization during repeated assays. This research could shed light on fatty acid metabolism pathways in staphylococcal species and clarify how this enzyme processes bacterial lipids.
2. Comparative Enzyme Studies Across Microbial Species
The purified protein works well as a reference enzyme when comparing oleate hydratase activity between different bacterial species. Scientists can examine substrate preferences, optimal reaction conditions, and catalytic efficiency, contrasting this Macrococcus enzyme with oleate hydratases from other microorganisms. The standardized recombinant format enables controlled comparative analyses that may reveal evolutionary relationships and functional diversity within the oleate hydratase enzyme family.
3. Antibody Development and Immunological Studies
Scientists can use the recombinant protein as an immunogen to create specific antibodies against Macrococcus caseolyticus oleate hydratase. The purified protein offers a well-defined antigen for immunization protocols in laboratory animals or for in vitro antibody selection methods. These antibodies could become valuable research tools for detecting this enzyme in bacterial cell extracts, investigating its cellular location, or developing immunoassays focused on Macrococcus metabolism research.
4. Protein-Protein Interaction Studies
Researchers can use the 6xHis-tagged recombinant protein in pull-down assays to find potential protein partners that interact with oleate hydratase in Macrococcus caseolyticus. Using the tagged protein as bait with bacterial cell lysates or purified protein libraries might uncover regulatory proteins or metabolic pathway components that associate with this enzyme. These interaction studies could reveal how cells regulate fatty acid metabolism and how oleate hydratase activity fits into larger metabolic networks.
