Recombinant Staphylococcus aureus 30 kDa neutral phosphatase gets produced in E.coli and comes with an N-terminal 6xHis-SUMO tag that helps with purification and appears to boost stability. This partial protein covers the 1-35 amino acid region and reaches over 90% purity, which SDS-PAGE analysis confirms. It's designed strictly for research purposes and seems to offer a dependable, high-quality choice for studies that need this particular phosphatase.
The 30 kDa neutral phosphatase from Staphylococcus aureus is an enzyme that likely plays a key role in phosphate metabolism. Phosphatases are important for many cellular processes - signal transduction and energy metabolism among them - by removing phosphate groups from substrates. Studying this enzyme may provide insights into bacterial physiology and potential interactions within host environments. This makes it a potentially valuable tool in microbiological and biochemical research.
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.
Staphylococcus aureus 30 kDa neutral phosphatase is a bacterial enzyme that requires precise folding, proper active site formation, and specific tertiary structure for its functional phosphatase activity. The E. coli expression system is homologous to this bacterial protein, which increases the probability of correct folding. However, the partial fragment (1-35aa) represents only a small N-terminal portion of the full-length protein and lacks critical catalytic domains essential for enzymatic activity. The large N-terminal 6xHis-SUMO tag (∼15 kDa) is significantly larger than the protein fragment itself (∼4 kDa), creating severe steric interference that will completely disrupt any potential functional domains. The probability of correct folding with functional phosphatase activity is essentially zero.
1. Antibody Development and Epitope Mapping
This application has severe limitations. While antibodies can be generated, the immune response will primarily target the large foreign SUMO tag rather than the small phosphatase fragment. Antibodies may not recognize the full-length, properly folded phosphatase in its native context.
2. Structural and Biochemical Characterization Studies
Basic biophysical analysis can be performed but will primarily reflect SUMO tag properties rather than phosphatase structure. The 35aa fragment is too short to form any meaningful phosphatase domain structure. Results will describe a tag-dominated protein rather than native phosphatase characteristics.
Final Recommendation & Action Plan
This SUMO-tagged phosphatase fragment is fundamentally unsuitable for any meaningful phosphatase research due to the extreme size disparity between the tag (15 kDa) and the protein fragment (4 kDa). The SUMO tag is nearly four times larger than the phosphatase fragment itself, making all functional and interaction studies biologically irrelevant. The only limited application is generating tag-specific antibodies (Application 1 with severe limitations). Avoid all interaction, structural, and binding studies entirely. For reliable phosphatase research, use full-length protein constructs that contain the complete catalytic domain and functional regions, preferably with minimal tags to preserve native structure and function.
