Recombinant Mouse Transcription factor MafK is expressed in a mammalian cell system, which appears to ensure proper folding and post-translational modifications. The protein comes as a full-length construct covering amino acids 1-156. It includes an N-terminal 10xHis tag and a C-terminal Myc tag for purification and detection purposes. SDS-PAGE analysis shows purity exceeds 85%, making it suitable for various research applications.
MafK belongs to the small Maf transcription factor family and is known for forming heterodimers with larger basic leucine zipper proteins. The protein likely plays a role in regulating gene expression by binding to DNA and influencing pathways such as oxidative stress response and cellular differentiation. Given its function in transcriptional regulation, MafK represents an important target for studies examining gene expression and cellular processes.
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-tag design—N-terminal 10xHis and C-terminal Myc—makes purification and detection of MafK protein complexes straightforward. Researchers can immobilize the recombinant MafK on nickel-affinity resins to capture potential binding partners from cell lysates or purified protein libraries. This dual-tag approach offers flexibility: the His-tag handles capture while the Myc-tag manages detection within the same experiment. Such studies may help identify transcription factor complexes and co-regulatory proteins, particularly those involved in MafK's transcriptional regulation networks.
2. Antibody Development and Validation
Since the protein is expressed in mammalian cells, it maintains proper folding and post-translational modifications that make it a reasonable immunogen for antibody production. The 85% purity level should be sufficient for generating specific antibodies against mouse MafK in most research contexts. The dual tags serve as useful internal controls when testing antibody specificity—researchers can distinguish between antibodies that recognize the native protein versus those targeting tag sequences. This recombinant protein works well as both a positive control and standard in antibody validation experiments.
3. ELISA-Based Quantitative Assays
The C-terminal Myc tag opens up possibilities for developing sandwich ELISA assays to detect and quantify MafK protein levels in experimental samples. The recombinant protein can function as a calibration standard with known concentrations for generating standard curves. Because it's produced in mammalian cells, the protein likely maintains native-like conformational epitopes that antibodies raised against endogenous MafK would recognize. This becomes particularly useful when studying MafK expression levels across different cell types or under varying experimental conditions.
4. Biochemical Characterization and Stability Studies
The purified recombinant MafK allows for detailed biochemical analysis, including molecular weight confirmation, thermal stability assessment, and buffer optimization studies. Having dual tags provides multiple detection methods for monitoring protein integrity under various experimental conditions. Scientists can examine how the protein behaves under different pH, salt, and temperature conditions to optimize both storage and experimental protocols. While the 85% purity may not meet requirements for structural determination studies, it appears adequate for most standard biochemical characterization experiments.
