Recombinant Mouse Kallikrein 1-related peptidase b22 (Klk1b22) gets produced in an E.coli expression system and contains amino acids 25-259 of the mature protein. The protein comes with an N-terminal 6xHis-SUMO tag, which makes purification and solubility much more manageable. SDS-PAGE analysis shows it reaches over 90% purity - pretty solid for most research work.
Klk1b22 belongs to the kallikrein-related peptidase family, a group known for proteolytic activity across different physiological processes. These enzymes appear to play important roles in inflammation pathways, blood pressure regulation, and tissue remodeling. Though the functional dynamics of Klk1b22 may provide insights into these critical biological processes, much about its specific role remains to be fully understood.
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. Antibody Development and Immunoassay Optimization
This recombinant Klk1b22 protein works well as an immunogen for creating specific antibodies against mouse kallikrein 1-related peptidase b22. That N-terminal 6xHis-SUMO tag makes purification straightforward and helps with immobilization during antibody screening assays. The >90% purity should be sufficient for producing decent antibodies with minimal cross-reactivity issues. Researchers could then use these antibodies in Western blotting, immunoprecipitation, or ELISA-based detection systems when studying Klk1b22 expression in mouse tissues and cell lines.
2. Protein-Protein Interaction Studies Using Tag-Assisted Pull-Down Assays
That N-terminal 6xHis-SUMO tag opens up possibilities for metal affinity-based pull-down experiments to hunt for potential binding partners of Klk1b22. Scientists can immobilize the protein on nickel-charged resin, then incubate it with mouse tissue lysates or cell extracts to capture whatever might be interacting. Mass spectrometry analysis of co-precipitated proteins could help map the Klk1b22 interactome. This approach seems particularly useful since the biological activity hasn't been tested yet - interaction studies might offer a more practical research direction.
3. Biochemical Characterization and Stability Studies
This recombinant protein gives researchers a standardized tool for investigating Klk1b22's biochemical properties, including thermal stability, pH tolerance, and buffer compatibility. Teams can run differential scanning fluorimetry, dynamic light scattering, and analytical size exclusion chromatography to characterize protein folding and aggregation behavior. The mature protein region (25-259aa) expressed in E.coli allows for cost-effective production of the material needed for extensive biochemical profiling experiments.
4. Comparative Structural and Functional Analysis Within Kallikrein Family
The recombinant Klk1b22 proves useful in comparative studies alongside other kallikrein family members to understand evolutionary relationships and structural differences. Cross-reactivity studies with antibodies raised against related kallikreins may provide insights into conserved epitopes and antigenic regions. The protein can also serve as a negative control in enzymatic assays designed for other kallikrein family members, which helps establish specificity profiles for various substrates and inhibitors.
