Creative Biostructure can provide advanced custom Mempro™ immunoglobulin-like superfamily (E set) protein production services in virus-like particles system.
Virus-like particles (VLPs) can mimic the native virus, but are non-infectious owing to they do not have any viral genetic materials. VLPs are self-assembly multiprotein structures, which are widely used in the field of vaccinology. It has proven that virus-like particles carrying conformationally-complex membrane proteins (termed lipoparticles) can be applied for integral membrane protein production. Lipoparticles can incorporate a large variety of structurally intact membrane proteins, including G protein-coupled receptors (GPCRs) and ion channels. Members of the immunoglobulin superfamily (IgSF) have an Ig domian, which possesses an Ig-like fold that composed of approximately 70-100 amino acids in anti-parallel β-strands. Immunoglobulin-like superfamily termed E set, includes a wide range of domains that have an Ig-like fold. E set also includes several fibronectin type III domain-containing families.
Figure 1. The structural model of AP-2 complex.
Virus-like particles can be applied for a large variety of applications, including:
Creative Biostructure offers high-quality E set proteins in the stable, highly purified and native-conformation state. Lipoparticles can be generated from bacterial cells, yeast cells, insect cells, plant cells and mammalian cells for E set protein production. Well-characterized E. coli strains and insect cells are the most popularly used systems for VLPs production. Mammalian cells are also widely used for VLPs production. We can obtain lipoparticles from mammalian cells by co-expressing the retroviral structural core polyprotein, Gag, along with a desired membrane protein. Gag core proteins self-assemble at the plasma membrane, where they bud off and capture receptor-type kinases. Since the E set proteins within lipoparticles are derived directly from the cell surface without mechanical disruption or detergents, the native structure and orientation of membrane proteins are preserved.
Creative Biostructure can offer other various Mempro™ membrane protein production services. Please feel free to contact us for a detailed quote.
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G. Bodelón, et al. (2013). Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies. FEMS Microbiol. Rev., 37(2): 204-250.
Immunoglobulin-like superfamily (E set). Orientations of proteins in membranes. (OPM). (http://opm.phar.umich.edu/families.php?superfamily=99)
P. Roy, et al. (2009). Prospects for improved bluetongue vaccines. Nat. Rev. Microbiol., 7: 120-128.
S. Willis, et al. (2008). Virus-like particles as quantitative probes of membrane protein interactions. Biochemistry, 47(27): 6988-6890.