Recombinant Mouse Methylmalonyl-CoA mutase, mitochondrial (Mutc) is expressed in E.coli and covers the full length of the mature protein from amino acids 31 to 748. The protein carries an N-terminal 6xHis tag, which makes purification and detection more straightforward. Purity exceeds 90% according to SDS-PAGE verification, though this should provide reliable results for most experimental applications. This product is intended for research use only.
Methylmalonyl-CoA mutase plays a crucial role in cellular metabolism—specifically converting methylmalonyl-CoA to succinyl-CoA. This conversion appears vital for breaking down certain amino acids and fatty acids. The enzyme's activity seems essential for metabolic pathways that keep normal cellular function intact. Given this central role, Mutc has become a significant focus in metabolic research. Scientists are using it to better understand energy production and various metabolic disorders.
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. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays
The N-terminal 6xHis-tag allows researchers to immobilize this recombinant mouse methylmalonyl-CoA mutase on nickel-affinity resins for pull-down experiments. Scientists can then investigate potential binding partners or cofactors that may interact with the mitochondrial enzyme. This involves incubating the immobilized protein with cell lysates or purified protein candidates. The >90% purity level should be sufficient for identifying specific interactions while reducing non-specific binding from contaminants. This approach might help clarify the protein's role in metabolic pathways and reveal regulatory mechanisms.
2. Antibody Development and Validation
The high purity (>90%) and full-length mature protein sequence (31-748aa) suggest this recombinant protein could work well for immunizing laboratory animals. Researchers can generate polyclonal or monoclonal antibodies against mouse methylmalonyl-CoA mutase this way. The resulting antibodies can then be validated using the same recombinant protein in Western blot, ELISA, or immunoprecipitation assays. The His-tag makes purification and immobilization easier for antibody screening and characterization experiments.
3. Biochemical Characterization and Cofactor Binding Studies
This recombinant protein may be useful for investigating the biochemical properties of mouse methylmalonyl-CoA mutase. Studies could examine cofactor requirements, optimal buffer conditions, and stability parameters. Researchers can perform binding assays to study interactions with known cofactors such as adenosylcobalamin (vitamin B12). They might also examine how the protein responds to different pH and salt conditions. The E. coli expression system appears to provide sufficient protein yield for multiple experimental conditions and replicates.
4. Comparative Species Analysis
The mouse-specific sequence (Mus musculus) makes comparative studies with methylmalonyl-CoA mutases from other species possible. Researchers can identify conserved regions and species-specific differences this way. Scientists might use this protein alongside human or other mammalian orthologs to study evolutionary relationships, structural differences, or functional variations. The standardized expression system and purification approach should allow for consistent comparison across different species variants.
