Recombinant Mouse Extracellular tyrosine-protein kinase PKDCC (Pkdcc) is expressed in a baculovirus system, spanning the full length of the mature protein from amino acids 33 to 492. The protein includes an N-terminal 10xHis-tag and a C-terminal Myc-tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows purity exceeding 85%, suggesting it's well-suited for various research applications.
Extracellular tyrosine-protein kinase PKDCC appears to play a crucial role in cellular signaling pathways. The protein is known for its kinase activity and participates in phosphorylation processes that regulate various cellular functions. Studying this protein may be important for understanding signal transduction mechanisms and its potential involvement in cellular development and differentiation processes. Researchers use this protein to explore its functions and interactions within these biological pathways.
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 Pull-Down Assays
The dual-tagged recombinant PKDCC protein with N-terminal His-tag and C-terminal Myc-tag provides useful tools for investigating protein-protein interactions. Pull-down experiments can take advantage of the His-tag by immobilizing the protein on nickel-affinity resins to identify potential binding partners from mouse cell lysates or tissue extracts. Meanwhile, the Myc-tag allows for straightforward detection and confirmation of protein capture through Western blotting or immunofluorescence techniques. This approach may help clarify the molecular networks and signaling pathways involving PKDCC in cellular processes.
2. Antibody Development and Validation
This recombinant mouse PKDCC protein serves as a suitable immunogen and positive control for developing specific antibodies against PKDCC. The high purity (>85%) and proper folding from the baculovirus expression system likely ensure presentation of native epitopes for antibody generation. Both tags make purification monitoring easier and allow researchers to distinguish between antibodies recognizing the native protein versus the tags. Antibodies generated this way can be validated using this recombinant protein in various immunoassays including ELISA, Western blotting, and immunoprecipitation experiments.
3. Biochemical Characterization and Enzyme Kinetics Analysis
The recombinant PKDCC protein can be used for comprehensive biochemical characterization studies including protein stability, optimal buffer conditions, and temperature sensitivity. Researchers can investigate the protein's structural properties through techniques such as circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation. The purified protein also enables detailed kinetic studies to understand substrate specificity and catalytic parameters, providing fundamental insights into PKDCC's enzymatic properties and regulatory mechanisms.
4. Cell-Based Functional Assays and Overexpression Studies
This recombinant protein can be used in cell culture experiments to study PKDCC function through protein transduction or microinjection techniques. The Myc-tag makes it possible to track exogenous protein localization and expression levels in transfected cells through immunofluorescence microscopy. Researchers can investigate the effects of PKDCC overexpression on cellular phenotypes, signaling pathway activation, and gene expression profiles. The protein can also serve as a positive control in cell-based assays designed to study PKDCC-mediated cellular responses.
