469results about "Fusions for enhanced expression stability/folding" patented technology

Genetically-encodable, environmentally-responsive fusion proteins comprising ELP peptides. Such fusion proteins exhibit unique physico-chemical and functional properties that can be modulated as a function of solution environment. The invention also provides methods for purifying the FPs, which take advantage of these unique properties, including high-throughput purification methods that produce high yields (e.g., milligram levels) of purified proteins, thereby yielding sufficient purified product for multiple assays and analyses. The high throughput purification technique is simpler and less expensive than current commercial high throughput purification methods, since it requires only one transfer of purification intermediates to a new multiwell plate.

In certain aspects, the present invention provides compositions and methods for promoting bone growth and increasing bone density.

In certain aspects, the present invention provides compositions and methods for promoting bone growth and increasing bone density.

The present application is directed to stabilized HIV envelope glycoprotein trimers. The trimers are stabilized by introducing trimeric motifs, preferably the GCN4 coiled coil or the fibritin trimeric domain at certain sites, for example in the gp41 ectodomain. These stabilized trimers or DNA molecules encoding such trimers can be used to generate an immunogenic reaction. The trimers can also be used in assays to screen for molecules that interact with them—and to identify molecules that interact with specific sites.

Genetically-encodable, environmentally-responsive fusion proteins comprising ELP peptides. Such fusion proteins exhibit unique physico-chemical and functional properties that can be modulated as a function of solution environment. The invention also provides methods for purifying the FPs, which take advantage of these unique properties, including high-throughput purification methods.

The invention relates to fusion protein containing a fluorescent protein fragment and an application of the fusion protein. Specifically, the invention provides the fusion protein, and the fusion protein has a structure as shown in (P1-L1)s-A1-(X)n-A2-(L2-P2)t. (X)n or A1-(X)n in the fusion protein can promote the folding and expression of fusion target peptide, improve the solubility of the fusion protein and reduce the intermolecular interaction of the fusion protein, so that the fusion target peptide can be folded under the high concentration with commercial significance. (X)n or A1-(X)n inthe fusion protein can be digested into a plurality of oligopeptides of which the lengths are far less than the length of the target peptide, so that the separation of the oligopeptides from the target peptide is better facilitated, and the purification of the target peptide is more convenient.

A polypeptide and polynucleotides encoding same comprising one carboxy-terminal peptide (CTP) of chorionic gonadotrophin attached to an amino terminus of a cytokine and two carboxy-terminal peptides (CTP) of chorionic gonadotrophin attached to a carboxy terminus of a cytokine are disclosed. Pharmaceutical compositions comprising the polypeptide and polynucleotides of the invention and methods of using same are also disclosed.

Methods and compositions for the rapid and reversible destabilizing of specific proteins in vivo using cell-permeable, synthetic molecules are described.

Methods for enhancing expression levels and secretion of heterologous fusion proteins in a host cell are disclosed.

A heparin-binding protein having covalently bonded heparan sulfate sugar chains within its molecule is produced by ligating a cDNA encoding a peptide which can be modified with heparan sulfate sugar chains selectively to a cDNA encoding a heparin-binding protein and producing in an animal cell the gene product of the resultant ligated cDNA. This heparan sulfate sugar chain-modified heparin-binding protein is functionalized by covalently bonding thereto glycosaminoglycan sugar chains containing little chondroitin sulfate. For example, this heparin-binding protein is excellent in stabilities, such as thermostability, acid resistance, alkali resistance and in vivo stability. Further, the heparan sulfate sugar chain-modified heparin-binding protein is effective in cell proliferation and tissue regeneration, and has effect of regulating the physiological functions of FGFs. Thus, this heparin-binding protein is extremely useful as a medicine for preventing or treating various FGF-related diseases.