Recombinant Human Antithrombin-III (SERPINC1) is produced through a baculovirus expression system and contains the complete protein sequence spanning amino acids 1 to 464. The protein includes an N-terminal 6xHis tag, which simplifies the purification process. SDS-PAGE analysis confirms that purity levels exceed 85%. This product is designed for research use only and should not be used for diagnostic or therapeutic purposes.
Antithrombin-III appears to be one of the most important serine protease inhibitors in blood coagulation regulation. The protein primarily inhibits thrombin and several other enzymes within the coagulation cascade, which likely helps maintain proper hemostatic balance. Research involving this protein may provide valuable insights into coagulation disorders and anticoagulation strategies, particularly regarding how blood clotting mechanisms work and how they're controlled.
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. In Vitro Protein-Protein Interaction Studies
Researchers can use this recombinant human antithrombin-III to study how it interacts with various coagulation factors, especially thrombin and factor Xa, under controlled laboratory conditions. The N-terminal 6xHis tag allows for straightforward immobilization on nickel-coated surfaces during surface plasmon resonance experiments or similar binding assays. Scientists might examine binding kinetics and affinity constants, along with how heparin or other cofactors influence these interactions. These studies could help clarify the molecular mechanisms behind coagulation regulation at the protein level.
2. Antibody Development and Characterization
The purified recombinant protein works well as an antigen for creating monoclonal or polyclonal antibodies against human antithrombin-III. Since the protein maintains its full-length structure (1-464aa), antibodies can potentially target various epitopes throughout the entire protein. Scientists can then characterize these antibodies using the recombinant protein in ELISA, Western blot, or immunoprecipitation assays to assess specificity and cross-reactivity patterns.
3. Biochemical Structure-Function Analysis
This recombinant antithrombin-III proves useful in biochemical assays designed to examine the structural properties and conformational changes typical of serpin family proteins. Researchers might investigate protein stability under different conditions, analyze folding patterns, or examine how various buffer conditions or chemical modifications impact structure. The His-tag makes purification straightforward for subsequent analytical techniques like circular dichroism spectroscopy or dynamic light scattering.
4. Pull-Down Assays for Cofactor Identification
The N-terminal 6xHis tag makes this protein well-suited for nickel affinity-based pull-down experiments aimed at identifying potential binding partners or cofactors from cell lysates or plasma samples. Scientists can immobilize the recombinant antithrombin-III on nickel beads and use it as bait to capture interacting proteins. Mass spectrometry analysis can then identify these captured proteins. This approach may help discover previously unknown regulatory proteins or cofactors that influence antithrombin-III function.
5. Comparative Protein Analysis Studies
The recombinant protein can function as a reference standard when comparing antithrombin-III variants, mutants, or proteins from different expression systems in preclinical research. Scientists might use this baculovirus-expressed protein to establish baseline characteristics for comparative studies examining how genetic variants or post-translational modifications affect protein properties. The consistent expression system and purification method appears to provide a reliable control for such comparative analyses.
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