A method for producing Metal Organic Framework (MOF) having a framework that encapsulates a bio-molecule, the method comprising combining in a solution the bio-molecule and MOF precursors, wherein the bio-molecule promotes formation of the encapsulating framework. The method stems from a surprising effect that a bio-molecule can promote or trigger the formation of MOF when combined together in a solution with MOF precursors. That is, it has now been found that a bio-molecule can effectively act as a seed around which the framework forms, with the resulting framework encapsulating the bio-molecule.

The present invention relates to a hydrogel useful to promote neurotization, osteogenesis and angiogenesis.

The invention is directed to a complex, including: a porous composite carrier including: a porous organic foam material containing open pores, each pore comprising a wall defining the pore; and a crosslinked product having aldehyde groups and immobilized on the surface of the walls of one or more pores of the porous organic foam materials, and a protein, polypeptide, or oligopeptide immobilized onto the porous composite carrier through a reaction between an amino group of the protein, polypeptide or oligopeptide and an aldehyde group of the composite carrier. The immobilized product has high specific surface area and high specific activity. The immobilization is simple and in low cost, and is suitable for industrial application.

The invention is directed to a complex, including: a porous composite carrier including: a porous organic foam material containing open pores, each pore comprising a wall defining the pore; and a crosslinked product having aldehyde groups and immobilized on the surface of the walls of one or more pores of the porous organic foam materials, and a protein, polypeptide, or oligopeptide immobilized onto the porous composite carrier through a reaction between an amino group of the protein, polypeptide or oligopeptide and an aldehyde group of the composite carrier. The immobilized product has high specific surface area and high specific activity. The immobilization is simple and in low cost, and is suitable for industrial application.

Provided is an affinity chromatography carrier that maintains high immunoglobulin-binding capacity and high alkali resistance. An immunoglobulin-binding protein including at least one modified immunoglobulin-binding domain, the modified immunoglobulin-binding domain being a polypeptide consisting of an amino acid sequence of an immunoglobulin-binding domain selected from the group consisting of the B domain, Z domain, C domain, and variants thereof of Staphylococcus aureus protein A, in which at least one amino acid residue is inserted between positions corresponding to the 3-position and position 4 of the amino acid sequence of the B domain, Z domain or C domain.

Provided is an affinity chromatography carrier that maintains high immunoglobulin-binding capacity and high alkali resistance. An immunoglobulin-binding protein including at least one modified immunoglobulin-binding domain, the modified immunoglobulin-binding domain being a polypeptide consisting of an amino acid sequence of an immunoglobulin-binding domain selected from the group consisting of the B domain, Z domain, C domain, and variants thereof of Staphylococcus aureus protein A, in which at least one amino acid residue is inserted between positions corresponding to the 3-position and position 4 of the amino acid sequence of the B domain, Z domain or C domain.

The present invention provides a method for suppressing non-specific binding of a binding protein to a surface molecule of eukaryotic cell membrane or exosome, including immobilizing the binding protein on a carrier in the presence of gelatin.

A platform enabling the manufacture of thermostable vaccines by incorporating recombinantly expressed, viral envelope proteins in their native conformation into ether glycerophospholipid nanodisc structures that simulate the natural environment of the envelope proteins. The ether glycerophospholipids include ether-linked hydrophobic side chains, and are derived from or modeled after those found in thermophile bacteria, which increase thermostability, thereby significantly enhancing the vaccine's potency, enabling the production of highly multivalent vaccines incorporating multiple variants of the viral antigen, and improving stability and shelf-life.

A platform enabling the manufacture of thermostable vaccines by incorporating recombinantly expressed, viral envelope proteins in their native conformation into ether glycerophospholipid nanodisc structures that simulate the natural environment of the envelope proteins. The ether glycerophospholipids include ether-linked hydrophobic side chains, and are derived from or modeled after those found in thermophile bacteria, which increase thermostability, thereby significantly enhancing the vaccine's potency, enabling the production of highly multivalent vaccines incorporating multiple variants of the viral antigen, and improving stability and shelf-life.

the present invention provides a method for producing a protein having a supramolecular structure in which a bioactive substance is encapsulated, comprising: (I) bringing a subunit of a protein, which forms a supramolecular structure, a bioactive substance, and a solution for forming the protein having the supramolecular structure from the subunit into contact with one another in a flow micro mixer.