Recombinant Pig Integrin beta-1 (ITGB1) is expressed in E. coli and comprises the amino acid residues 140-378. This partial protein comes engineered with an N-terminal 10xHis-tag and a C-terminal Myc-tag, which helps with purification and detection. The protein shows purity greater than 85% as assessed by SDS-PAGE, ensuring reliable performance in research applications. This product is intended for research use only.
Integrin beta-1 (ITGB1) appears to be a crucial component of the integrin family, playing what seems to be a significant role in cell adhesion and signal transduction. It's involved in various biological processes, including extracellular matrix interactions and cellular responses to the environment. ITGB1 is likely essential for understanding cell movement, proliferation, and survival. This makes it a valuable target for research in cellular biology and pathology.
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. Protein-Protein Interaction Studies Using Pull-Down Assays
The dual-tagged recombinant pig ITGB1 fragment (140-378aa) can be immobilized on Ni-NTA beads through its N-terminal 10xHis tag to capture potential binding partners from cell lysates or purified protein libraries. This partial ITGB1 construct may well retain important binding domains that interact with extracellular matrix components, other integrin subunits, or intracellular signaling proteins. The C-terminal Myc tag provides an additional detection method for Western blot confirmation of the bait protein presence during pull-down experiments. Studies like these could potentially help identify novel binding partners specific to this region of pig ITGB1 or validate known interactions in a porcine model system.
2. Antibody Development and Epitope Mapping
This recombinant pig ITGB1 fragment can serve as an immunogen for generating species-specific antibodies against pig integrin beta-1. The 239-amino acid construct (140-378aa) represents a substantial portion of the protein that appears to contain multiple antigenic epitopes. Researchers can use this purified protein to immunize laboratory animals for polyclonal antibody production or as a screening antigen for monoclonal antibody development. The dual tags also make possible epitope mapping studies to distinguish between antibodies recognizing the native ITGB1 sequence versus those binding to the His or Myc tags.
3. Comparative Structural and Biochemical Analysis
The partial pig ITGB1 construct can be used in comparative studies examining structural and biochemical differences between porcine and other mammalian integrin beta-1 proteins. Researchers can perform biophysical characterization including circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to assess protein folding and stability. The high purity (>85%) makes this protein suitable for detailed biochemical analyses such as thermal stability assays or chemical cross-linking studies. Comparative analyses like these are valuable for understanding species-specific differences in integrin structure and for validating pig models in biomedical research.
4. ELISA-Based Binding Assays
The dual-tagged pig ITGB1 fragment can be used in enzyme-linked immunosorbent assays to study binding interactions with potential ligands or other proteins. The protein can be immobilized directly on ELISA plates or captured using anti-His or anti-Myc antibodies for oriented immobilization. This approach allows for quantitative assessment of binding affinities with extracellular matrix components, synthetic peptides, or other proteins that may interact with this specific region of ITGB1. The assay format appears particularly useful for screening compound libraries or testing the effects of mutations on binding interactions.
