Recombinant Human Vasculin (GPBP1) is produced in an E.coli expression system, covering amino acids 293-473 of the full protein. The protein carries an N-terminal 6xHis-SUMO tag to aid in purification and appears to enhance stability. SDS-PAGE analysis shows purity greater than 90%, which makes it appropriate for various research applications. This product is for research use only and is not intended for diagnostic or therapeutic purposes.
The GPBP1 gene encodes vasculin, which seems to play a role in transcriptional regulation and has been linked to modulating gene expression. It's involved in important pathways related to vascular development and function. Understanding this protein's activity and interactions may be essential for research focused on vascular biology and related fields, potentially offering insights into cellular processes and therapeutic targets.
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 N-terminal 6xHis-SUMO tag allows for efficient attachment of this GPBP1 fragment (293-473aa) to nickel-affinity resins during pull-down experiments. Scientists can incubate the attached protein with cell lysates or purified protein libraries to discover new binding partners of vasculin's C-terminal region. The high purity (>90%) likely ensures minimal background binding from contaminants. This method appears particularly useful for mapping interaction domains within the 293-473aa region of GPBP1.
2. Antibody Development and Epitope Mapping
This recombinant GPBP1 fragment may serve as an immunogen for creating antibodies specific to the 293-473aa region of human vasculin. The purified protein provides a well-defined antigen for immunization protocols in laboratory animals. The same protein can then be used in ELISA-based screening to identify antibodies with high specificity and affinity. The His-SUMO tag makes purification and attachment straightforward during antibody validation assays.
3. Structural and Biophysical Characterization Studies
The high-purity recombinant protein appears suitable for biophysical analyses including circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation to examine the folding and oligomerization properties of this GPBP1 domain. Nuclear magnetic resonance or X-ray crystallography studies might provide structural insights into the 293-473aa region. If native protein structure is required for these analyses, the SUMO tag can be removed using SUMO protease.
4. In Vitro Functional Assays and Biochemical Analysis
This GPBP1 fragment can be used to explore the biochemical properties and potential enzymatic activities of vasculin's C-terminal domain under controlled in vitro conditions. Scientists can conduct substrate binding assays, thermal stability studies, and pH optimization experiments to characterize how the protein behaves. The His tag allows for easy protein recovery and reuse across multiple experimental conditions, which could make it cost-effective for extensive biochemical characterization studies.
