Recombinant Human Apolipoprotein B-100 (APOB) is produced in a yeast expression system, covering amino acids 28 to 127. This partial protein includes an N-terminal 6xHis tag to make purification and detection easier. The product achieves greater than 90% purity, as confirmed by SDS-PAGE analysis, which suggests it's reliable for research applications. This product is designed for research use only.
Apolipoprotein B-100 appears to be a crucial component of low-density lipoproteins (LDL) and plays a significant role in lipid transport and metabolism. It's essential for assembling and secreting very low-density lipoproteins (VLDL) and is integral to maintaining LDL particle structure. Understanding APOB's function may be vital for studies related to lipid disorders and cardiovascular research.
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. Antibody Development and Validation
This N-terminal fragment of human APOB (amino acids 28-127) can work as an immunogen or screening antigen for developing antibodies specific to the N-terminal region of apolipoprotein B-100. The recombinant protein's high purity (>90%) and His-tag likely make it suitable for immunization protocols and subsequent antibody characterization assays. Researchers can use this fragment in ELISA-based screening to identify monoclonal or polyclonal antibodies with specificity for this particular APOB region. The yeast expression system may provide proper eukaryotic protein folding while avoiding potential cross-reactivity issues that sometimes arise from bacterial expression systems.
2. Protein-Protein Interaction Studies
The His-tagged APOB fragment can be used in pull-down assays to investigate potential binding partners that interact with the N-terminal region of apolipoprotein B-100. The 6xHis tag allows efficient immobilization on nickel-based affinity matrices for capturing interacting proteins from cell lysates or purified protein preparations. This approach is particularly valuable for studying early steps in lipoprotein assembly or identifying novel regulatory proteins that may bind to this specific APOB domain. The defined amino acid range (28-127) provides a focused tool for mapping interaction sites within the larger APOB protein.
3. Structural and Biochemical Characterization
This recombinant APOB fragment works as a model system for investigating the structural properties and biochemical behavior of the N-terminal region of human apolipoprotein B-100. Researchers can perform biophysical analyses such as circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to characterize the protein's secondary structure, aggregation state, and stability. The high purity level makes it suitable for detailed biochemical studies including thermal stability assays and chemical cross-linking experiments. These studies may provide insights into the folding and structural organization of this specific APOB domain.
4. ELISA-Based Quantitative Assays
The His-tagged APOB fragment can function as a standard or capture antigen in enzyme-linked immunosorbent assays designed to detect and quantify APOB-related proteins or antibodies in research samples. The N-terminal His tag allows oriented immobilization on ELISA plates through metal chelate interactions, potentially improving assay reproducibility and sensitivity. This application is useful for researchers studying APOB expression levels, protein modifications, or immune responses in various experimental models. The defined fragment size allows for development of region-specific assays that focus on the N-terminal domain of APOB.
