Recombinant Mouse Tumor Necrosis Factor (Tnf) is produced in E. coli and comprises a partial sequence of amino acids 89 to 235. This tag-free protein demonstrates a purity greater than 95% as confirmed by SDS-PAGE analysis. It exhibits biological activity with an ED50 of 2-8 pg/ml in a cytotoxicity assay using L929 mouse fibroblast cells, alongside actinomycin D. The endotoxin level is maintained below 1.0 EU/µg as determined by the LAL method.
Tumor necrosis factor (TNF) appears to be one of those pivotal cytokines that somehow manages to wear many hats in the immune system. It's deeply involved in systemic inflammation and serves as part of the body's acute phase response. TNF plays what seems to be a crucial role in regulating immune cells, inducing fever, triggering apoptotic cell death, and inhibiting both tumorigenesis and viral replication. Given its broad influence, TNF has become integral to research spanning immunology, cancer studies, and various inflammatory diseases—making it a significant target for therapeutic research and drug development.
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. Cytotoxicity Assays for TNF-α Research
This recombinant mouse TNF protein works well as a positive control or standard in cytotoxicity assays. The L-929 mouse fibroblast cell system with actinomycin D, as validated by the activity testing method, appears particularly suitable for this purpose. With its defined ED50 range of 2-8 pg/ml, researchers get a reliable reference point for dose-response studies. Scientists can apply this protein to investigate TNF-α-mediated cell death mechanisms and validate experimental protocols for cytotoxicity screening.
2. In Vitro Inflammatory Response Studies
The biologically active mouse TNF protein may serve as an excellent tool for studying inflammatory pathways in mouse cell culture systems. Scientists can apply this protein to stimulate various mouse cell types, then examine downstream signaling cascades, gene expression changes, and inflammatory mediator production. The high purity (>95%) and low endotoxin levels (<1.0 EU/μg) suggest that observed effects should be specifically attributable to TNF-α activity rather than contaminating factors.
3. Antibody Development and Validation
This tag-free recombinant mouse TNF protein can work as an immunogen for generating anti-mouse TNF antibodies or as a standard for validating existing ones. The protein's high purity makes it suitable for immunization protocols, while its confirmed biological activity allows for functional validation of neutralizing antibodies. Scientists can apply this protein in competitive binding assays, ELISA development, and antibody specificity testing.
4. Protein-Protein Interaction Studies
The recombinant mouse TNF protein can be applied in biochemical assays to study its interactions with TNF receptors or other binding partners. Given its biological activity, this protein likely maintains proper folding necessary for receptor binding studies using techniques such as surface plasmon resonance, bio-layer interferometry, or co-immunoprecipitation assays. The tag-free nature of the protein eliminates potential interference from fusion tags in binding studies.
5. Preclinical Research Model Development
This biologically active mouse TNF protein may serve as a research tool for developing and validating mouse models of TNF-α-mediated pathological conditions in laboratory settings. Scientists can apply this protein to establish dose-response relationships, optimize experimental protocols, and serve as a positive control in studies examining TNF-α signaling pathways. The defined activity range provides a starting point for determining appropriate concentrations in various experimental paradigms.
