Recombinant Human Insulin-like growth factor I (IGF1) is produced in a yeast expression system and corresponds to the full length of the mature protein, spanning amino acids 49 to 118. This product carries an N-terminal 6xHis tag, which makes purification and detection more straightforward. SDS-PAGE analysis shows a purity level of greater than 90%, which appears suitable for various research applications requiring high-quality protein.
Insulin-like growth factor I (IGF1) represents a crucial protein in cell growth, development, and metabolism. It plays a significant role in regulating growth hormone activity and is integral to various signaling pathways that control cellular proliferation and differentiation. Given these pivotal functions, IGF1 has become extensively studied in fields like endocrinology and oncology, offering valuable insights into growth-related processes and diseases.
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. IGF1 Receptor Binding Studies
This recombinant human IGF1 can be used to investigate binding kinetics and affinity between IGF1 and its cognate receptor (IGF1R) as well as insulin receptor isoform A (IR-A) through surface plasmon resonance or fluorescence polarization assays. The N-terminal 6xHis tag allows for easy immobilization on nickel-coated surfaces during real-time binding analysis. Such studies may help clarify the molecular basis of IGF1-receptor interactions and could be useful for screening potential receptor modulators. The high purity (>90%) is likely to ensure reliable and reproducible binding data with minimal interference from contaminants.
2. Cell Proliferation and Survival Assays
The recombinant IGF1 protein can serve as either a positive control or treatment agent in cell culture experiments examining growth factor-dependent cellular responses. Researchers can apply this protein to stimulate various cell lines and primary cells, allowing them to study IGF1-mediated proliferation, differentiation, or survival pathways under controlled in vitro conditions. The yeast expression system offers a eukaryotic folding environment that may preserve native-like protein structure important for biological recognition. Meanwhile, the 6xHis tag makes purification and quantification straightforward for dose-response studies.
3. Antibody Development and Validation
This purified recombinant IGF1 can work as an immunogen for generating specific antibodies against human IGF1 or as a standard for validating existing anti-IGF1 antibodies. The protein can function in ELISA-based assays, Western blot controls, or immunoprecipitation experiments to assess antibody specificity and cross-reactivity. The N-terminal His tag provides an additional epitope that can be leveraged for detection or purification purposes in antibody characterization studies. High purity levels suggest that antibodies developed will have minimal cross-reactivity with contaminating proteins.
4. Protein-Protein Interaction Studies
The 6xHis-tagged IGF1 can be applied in pull-down assays to identify and characterize IGF1-binding proteins or potential interacting partners in cell lysates or purified protein preparations. The His tag allows for immobilization on nickel-affinity matrices, helping researchers capture IGF1-interacting proteins for subsequent mass spectrometry analysis or biochemical characterization. This approach may help map the IGF1 interactome and discover novel regulatory proteins or binding partners. The recombinant nature of the protein is likely to ensure consistent results across different experimental batches.
5. Structural and Biophysical Characterization
This recombinant IGF1 protein can be applied in structural biology studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to understand IGF1 structure and conformational dynamics. The protein can also work in biophysical analyses such as dynamic light scattering, analytical ultracentrifugation, or thermal stability assays to characterize its oligomerization state and stability properties. The yeast expression system may provide post-translational modifications that influence protein folding and stability. High purity levels appear essential for obtaining high-quality structural data and reliable biophysical measurements.
