Recombinant Human SPARC protein is produced in E. coli and spans the 18-303 amino acid region. This tag-free protein achieves purity levels greater than 98% as confirmed by SDS-PAGE. The protein remains fully biologically active, showing an ED50 of less than 3.0 µg/mL when inhibiting growth of Mv1Lu mink lung epithelial cells—this suggests a specific activity of over 333 IU/mg. Endotoxin levels stay below 1.0 EU/µg, as measured by the LAL method.
SPARC, or Secreted Protein Acidic and Rich in Cysteine, is a matricellular protein that participates in several biological processes. These include cell-matrix interactions and tissue remodeling. It appears to play a critical role in modulating cell adhesion, proliferation, and migration. This makes SPARC an important subject for studies examining extracellular matrix dynamics and cellular signaling pathways. Its significance in these areas likely makes it a valuable research tool for cell biology and tissue engineering work.
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. Cell Growth Inhibition Assays for Cancer Research
This recombinant SPARC protein may prove useful for studying cell growth inhibition mechanisms across various cancer cell lines, particularly given its validated activity against Mv1Lu mink lung epithelial cells. Researchers could establish dose-response curves to determine ED50 values for different cell types and compare how sensitive each line is to treatment. The high purity (>98%) and defined specific activity (>333 IU/mg) make it well-suited for quantitative studies examining SPARC's anti-proliferative effects. Low endotoxin levels help ensure that any observed growth inhibition stems from SPARC activity rather than inflammatory responses.
2. Extracellular Matrix Interaction Studies
SPARC is known to interact with various extracellular matrix components. This recombinant protein could be used in binding assays to characterize these interactions more thoroughly. Surface plasmon resonance, ELISA-based binding assays, or co-precipitation experiments might help researchers study SPARC's affinity for collagen, fibronectin, and other matrix proteins. Since this protein lacks fusion tags, there's less risk of interference in binding studies. Such experiments may help clarify SPARC's role in matrix remodeling and tissue architecture.
3. Anti-SPARC Antibody Development and Validation
This highly pure recombinant SPARC protein appears to be an excellent candidate for both immunogen and standard applications when developing anti-SPARC antibodies. Researchers could use the protein in immunization protocols to generate monoclonal or polyclonal antibodies, then rely on it as a positive control for Western blotting, immunohistochemistry, and ELISA work. The defined biological activity offers an additional functional readout for antibody neutralization studies. Consistent purity and activity likely make it suitable for establishing standardized antibody validation protocols.
4. Protein-Protein Interaction Screening
The biologically active recombinant SPARC could work well in pull-down assays and co-immunoprecipitation experiments designed to identify novel protein binding partners. Researchers might use this protein as bait in affinity chromatography or yeast two-hybrid screens to discover previously unknown SPARC interactors. High purity should minimize background binding, while the confirmed biological activity suggests proper protein folding necessary for physiologically relevant interactions. These studies may reveal new molecular pathways where SPARC participates in cellular processes.
5. Wound Healing and Tissue Repair Model Studies
Given SPARC's established role in tissue remodeling, this recombinant protein could be valuable for in vitro wound healing assays and tissue culture models. Researchers might add defined concentrations of SPARC to scratch assays, transwell migration studies, or organotypic cultures to examine how it affects cell migration and tissue repair processes. The quantified biological activity allows for precise dosing in these experimental systems. Low endotoxin content makes it appropriate for sensitive primary cell culture applications where inflammatory responses need to be minimized.
