Recombinant Mouse Granulocyte-macrophage colony-stimulating factor (Csf2) is produced in a mammalian cell expression system, which appears to ensure proper protein folding and post-translational modifications. The protein comprises the full length of the mature form, spanning amino acids 18 to 141, and is tagged with a C-terminal 6xHis-tag for ease of purification. With a purity greater than 95% as determined by SDS-PAGE, this product exhibits biological activity, evidenced by an ED50 of 40-170 pg/ml in a cell proliferation assay using PDC-P1 cells. Endotoxin levels are maintained below 1.0 EU/µg as determined by the LAL method.
Granulocyte-macrophage colony-stimulating factor (GM-CSF) represents a crucial cytokine involved in hematopoiesis. It's particularly important in the differentiation and proliferation of granulocyte and macrophage progenitor cells. GM-CSF also plays a significant role in immune responses and inflammation by modulating leukocyte functions. Given these properties, GM-CSF has become a protein of considerable interest in research exploring immune system regulation, inflammatory diseases, and potential therapeutic applications.
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. Cell Proliferation and Viability Assays for Hematopoietic Research
This recombinant mouse GM-CSF can be used to stimulate proliferation of granulocyte and macrophage progenitor cells in controlled in vitro experiments. The established ED50 range of 40-170 pg/ml using PDC-P1 cells provides what appears to be a validated starting point for dose-response studies. Researchers might apply this protein to investigate hematopoietic cell differentiation pathways, optimize culture conditions for primary bone marrow cells, or study the molecular mechanisms underlying GM-CSF-mediated cell survival and proliferation.
2. Cytokine Receptor Binding and Signaling Studies
The biologically active recombinant protein may serve as an ideal tool for investigating GM-CSF receptor interactions and downstream signaling cascades. Scientists can perform receptor binding assays, competition studies, and signal transduction pathway analysis using this standardized protein preparation. The high purity (>95%) and low endotoxin levels should ensure reliable results in sensitive biochemical assays examining JAK-STAT pathway activation or other GM-CSF-induced cellular responses.
3. Antibody Development and Validation
The C-terminal 6xHis tag appears to simplify purification and immobilization of this GM-CSF protein for antibody screening and characterization applications. Researchers can use this protein as an antigen for developing mouse GM-CSF-specific antibodies or as a positive control in immunoassays. The mammalian expression system likely ensures proper protein folding and post-translational modifications, making it suitable for generating antibodies that recognize native GM-CSF conformations.
4. Comparative Species-Specific Cytokine Studies
This mouse-specific GM-CSF enables researchers to conduct comparative studies examining species differences in cytokine function and receptor specificity. The protein can be used alongside human or other species variants to investigate evolutionary conservation of GM-CSF signaling pathways. Such studies may be particularly valuable for validating mouse models in preclinical research and understanding species-specific responses to cytokine stimulation.
5. Protein-Protein Interaction and Pull-Down Assays
The 6xHis tag enables efficient capture of this GM-CSF protein using nickel-based affinity matrices for pull-down experiments. Researchers can investigate direct protein interactions between GM-CSF and its receptors or other binding partners using this tagged protein. The high purity and biological activity suggest that observed interactions should reflect genuine molecular associations rather than artifacts from protein aggregation or misfolding.
