Recombinant Mouse Insulin-like growth factor-binding protein 1 (Igfbp1) is produced in an E. coli expression system and contains the full-length mature protein sequence from amino acids 26 to 272. The protein includes an N-terminal 6xHis-SUMO tag that makes purification and detection more straightforward. SDS-PAGE analysis shows the product achieves greater than 90% purity, which appears suitable for demanding research applications.
Insulin-like growth factor-binding protein 1 (IGFBP1) seems to play an important role in controlling insulin-like growth factor (IGF) activity through high-affinity binding interactions. The protein likely influences growth and metabolic processes by regulating how much IGF remains available to cells. Research into developmental biology and endocrine function has focused considerable attention on this protein.
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.
Mouse Igfbp1 is a secreted protein that requires complex disulfide bond formation and proper tertiary structure for its biological function of binding insulin-like growth factors (IGFs). The E. coli expression system cannot perform the necessary post-translational modifications (particularly proper disulfide bonding) that are critical for Igfbp1's native conformation. While the SUMO tag may improve solubility, the protein is highly unlikely to achieve the correct folding needed for functional IGF-binding activity. Therefore, this recombinant protein is probably misfolded and inactive.
1. Antibody Development and Validation
This recombinant Igfbp1 serves as an excellent immunogen for generating antibodies against linear epitopes of the protein. The full-length mature sequence ensures comprehensive epitope coverage. The His-SUMO tag facilitates purification and immunization procedures. However, antibodies may not efficiently recognize conformational epitopes on native Igfbp1.
2. Biochemical Characterization and Stability Studies
This is the essential first step to assess the protein's physical properties. Techniques like circular dichroism can analyze secondary structure content, while size-exclusion chromatography can determine oligomeric state and homogeneity. These analyses provide crucial data for understanding the protein's properties, regardless of functional status.
Final Recommendation & Action Plan
The E. coli expression system cannot produce a functional Igfbp1, limiting applications to non-functional uses. The immediate priority is Application 2 (Biochemical Characterization) to assess the protein's physical state. Application 1 (Antibody Development) can proceed immediately for generating linear epitope antibodies. Binding data with IGF-I/IGF-II would be unreliable since proper binding requires precise tertiary structure. Comparative binding studies require properly folded proteins from all species being compared. Using misfolded mouse Igfbp1 alongside other potentially functional IGFBP1 variants would yield meaningless evolutionary insights.
