Recombinant Mouse Ig kappa chain V-V region K2 is produced in E. coli, expressing the full length of the mature protein from amino acids 21 to 115. The protein comes with an N-terminal 10xHis-tag and a C-terminal Myc-tag, which appears to make it quite versatile for research work. SDS-PAGE analysis shows purity levels above 85%, suggesting it should work well for most experimental applications that need reliable recombinant protein standards.
The Ig kappa chain V-V region K2 belongs to the immunoglobulin light chain kappa family. These proteins seem to play a crucial role in adaptive immune responses - they're involved in recognizing antigens and form part of the antigen-binding sites on antibodies. Understanding how this protein works may be essential for anyone studying immune system mechanisms or developing therapeutic antibodies.
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. Immunoglobulin Variable Region Structure-Function Studies
This recombinant mouse protein could serve as a useful model for investigating how immunoglobulin variable domains fold and maintain their structure. The dual tags make purification straightforward and detection easier in biochemical assays that examine protein stability, thermal denaturation, and conformational changes. Scientists can study the basic properties of antibody variable regions without dealing with the added complexity of full-length immunoglobulin molecules. Using E. coli as the expression system appears to offer a cost-effective way to produce enough protein for biophysical studies.
2. Antibody Engineering and Development Research
This protein might work well as a reference standard or control when engineering antibodies, particularly for variable region optimization projects. Labs developing new antibody fragments or studying how variable domains interact could find this well-characterized construct helpful for comparative analysis. The His and Myc tags make purification and detection more manageable across different experimental setups - this seems especially valuable for screening assays and binding studies. It's likely to be particularly useful for researchers working on single-chain variable fragments (scFv) or similar antibody-derived constructs.
3. Protein-Protein Interaction Studies
The dual-tag design makes this recombinant protein an attractive option for pull-down assays and co-immunoprecipitation experiments aimed at finding potential binding partners of immunoglobulin variable regions. The N-terminal His tag allows for immobilization on metal affinity matrices, while the C-terminal Myc tag provides a way to detect and validate interactions. This setup could help researchers investigate how variable regions interact with other cellular components or synthetic molecules in controlled lab conditions.
4. Tag-Based Assay Development and Validation
This protein works well as a positive control for developing and validating detection systems based on His-tags and Myc-tags. Its known molecular weight and dual-tag setup make it suitable for optimizing ELISA protocols, Western blot conditions, and other immunodetection methods. Labs can use it to establish standard curves, check antibody specificity, and troubleshoot tag-based purification and detection protocols - though results may vary depending on specific experimental conditions.
