Recombinant Mouse Bnip3 is produced using an in vitro E.coli expression system in the lab, containing a partial sequence that spans amino acids 50 to 187. The protein includes an N-terminal 6xHis tag, which makes purification and detection much easier. Based on SDS-PAGE analysis, the product appears to have a purity level above 90%, suggesting it should be reliable for research work. This is strictly for research purposes - not for any human or animal treatments or diagnostic testing.
Bnip3 belongs to the Bcl-2 family and seems to play an important role in controlling both apoptosis and autophagy pathways. It's particularly known for its connection to mitochondrial dynamics and how cells respond when oxygen levels drop. Because of its function in programmed cell death, Bnip3 has become a key protein for scientists studying cell survival and death mechanisms. Research into this protein may provide valuable insights into various normal and disease-related processes.
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
This N-terminal 6xHis-tagged recombinant mouse Bnip3 protein (aa 50-187) can be attached to nickel-affinity resins to find and study potential binding partners. The partial protein construct likely retains important interaction domains that are involved in forming protein complexes. Scientists can mix the attached Bnip3 with cell lysates or purified proteins to examine direct binding interactions. The high purity (>90%) should minimize background interference in these studies.
2. Antibody Development and Validation
This recombinant mouse Bnip3 fragment could work as an immunogen for creating specific antibodies against the 50-187 amino acid region. The purified protein can then validate antibody specificity through ELISA, Western blot, or surface plasmon resonance assays. The His-tag makes purification and attachment straightforward when screening hybridoma clones or testing antibody cross-reactivity. This application appears particularly valuable for developing research tools to study natural Bnip3 expression and where it's located in cells.
3. Structural and Biophysical Characterization Studies
The recombinant Bnip3 protein fragment can be used in structural biology work, including circular dichroism spectroscopy, dynamic light scattering, and NMR studies to examine its folding properties and secondary structure. This defined amino acid region (50-187) represents a specific domain that can be studied separately from the full-length protein. These studies may reveal important structural features of this particular Bnip3 region and how stable it remains under different buffer conditions.
4. In Vitro Binding Competition Assays
The purified His-tagged Bnip3 fragment works well in competitive binding experiments to study the specificity and strength of interactions involving this protein region. Scientists can use this recombinant protein as a competitor in assays designed to disrupt or characterize binding between Bnip3 and other cellular components. The high purity and well-defined composition make it suitable for quantitative binding studies where precise protein concentrations are critical.
5. Biochemical Assay Development and Optimization
This recombinant mouse Bnip3 protein can serve as a positive control or standard in biochemical assays designed to study Bnip3-related pathways. The consistent quality and purity allow for reproducible assay conditions during method development and validation studies. Scientists can use this protein to establish detection limits, fine-tune assay conditions, and standardize protocols for studying Bnip3 function across various experimental systems.
