Abstract: The present disclosure relates to a highly stable basic fibroblast growth factor mutant, and a use thereof. More specifically, the present disclosure provides: a highly stable basic fibroblast growth factor (bFGF) mutant, in which two or more amino acids in an amino acid sequence of SEQ ID NO: 1 are substituted with serine and one or more amino acids are substituted with cysteine; a DNA base sequence encoding the bFGF mutant; an expression vector including the DNA base sequence; a transformant transformed by the expression vector; a method of producing the bFGF mutant; and a composition including the bFGF mutant as an active ingredient. According to the present disclosure, the bFGF mutant of the present disclosure has excellent stability in an aqueous solution state and excellent thermal stability, and thus it is possible to produce functional cosmetics and skin inflammation medicines which do not lose activity, unlike conventional wild-type bFGF products, even during distribution and storage.

Abstract: The present disclosure relates to a highly stable basic fibroblast growth factor mutant, and a use thereof. Specifically, the present disclosure provides: a highly stable basic fibroblast growth factor mutant, in which two or more amino acids in an amino acid sequence of SEQ ID NO.: 1 are substituted with serine and one or more amino acids are substituted with cysteine; a DNA base sequence encoding the bFGF mutant; an expression vector including the DNA base sequence; a transformant transformed by the expression vector; a method of producing the bFGF mutant; and a composition including the bFGF mutant as an active ingredient. According to the present disclosure, the bFGF mutant of the present disclosure has excellent stability in an aqueous solution state and excellent thermal stability, and thus it is possible to produce functional cosmetics and skin inflammation medicines which do not lose activity, even during distribution and storage.

Abstract: There are provided mutants prepared by changing a DNA base sequence and an amino acid sequence of an epidermal growth factor (EGF), in which a mutant EGF protein has excellent thermal stability and stability even in the state of an aqueous solution, and a gene encoding the protein are provided; a recombinant vector including the gene and a microorganism transformed by the recombinant vector are provided; a method of preparing the mutant EGF protein is provided; a cosmetic composition for accelerating the growth of skin cell and skin regeneration, including the protein, the gene, or the recombinant vector, is provided; and by preparing a product using the EGF mutant according to the present invention, it is possible to produce functional cosmetics, in which the activity thereof is maintained even during a distribution and storage process unlike the conventional wild-type EGF product.

Abstract: There are provided mutants prepared by changing a DNA base sequence and an amino acid sequence of an epidermal growth factor (EGF), in which a mutant EGF protein has excellent thermal stability and stability even in the state of an aqueous solution, and a gene encoding the protein are provided; a recombinant vector including the gene and a microorganism transformed by the recombinant vector are provided; a method of preparing the mutant EGF protein is provided; a cosmetic composition for accelerating the growth of skin cell and skin regeneration, including the protein, the gene, or the recombinant vector, is provided; and by preparing a product using the EGF mutant according to the present invention, it is possible to produce functional cosmetics, in which the activity thereof is maintained even during a distribution and storage process unlike the conventional wild-type EGF product.

Abstract: The present invention provides a method of producing polypeptide utilizing a fusion protein of A-B type in the following formula (I), by culturing transformed microorganism comprising DNA sequence encoding the desirable polypeptide; A-B (I). In the above formula (I), A is a fusion partner of 25 or more amino acid residues where aspartic and glutamic acid residues are incorporated to have a net negative charge of 30% or more, and B is the target protein to be produced. The target protein can be isolated from the fusion protein by employing enzymatic cleavage site etc. at the carboxyl-terminus of the fusion partner.

Abstract: The present invention relates to a method for producing a recombinant protein capable of increasing expression rate of a target protein and also improving solubility and folding of the expressed target protein using a modified protein disulfide isomerase (PDI) as a fusion partner, and an expression vector containing the modified PDI gene as a fusion partner. The method for preparing a recombinant protein using a modified PDI as a fusion partner according to the present invention may solve the problems concerning a low yield and solubility and folding that conventional fusion partners have, and be widely used for protein drug and industrial protein production.

Abstract: Disclosed is a method for improving folding efficiency and solubility of a target protein linked to a RNA-binding protein by using RNA molecule as a molecular chaperone, wherein the RNA molecule interacts with the RNA-binding protein. More particularly, the present invention discloses method for improving folding efficiency and solubility of a target protein by transformation of a host cell with a expression vector comprising a polynucleotide encoding the target protein linked to an RNA-binding protein; culturing the transformed host cell in an appropriate culture medium under the condition that an RNA molecule either resident inside the host cell or provided by cotransformation of the host cell with polynucleotide encoding the RNA molecule interacts with the RNA-binding protein; and purifying the soluble protein from host cell lysate. The method of the present invention is very useful for production of soluble proteins for therapeutic, prophylactic and diagnostic applications.

Abstract: The present invention relates to a method for producing a recombinant protein capable of increasing expression rate of a target protein and also improving solubility and folding of the expressed target protein using a modified protein disulfide isomerase (PDI) as a fusion partner, and an expression vector containing the modified PDI gene as a fusion partner. The method for preparing a recombinant protein using a modified PDI as a fusion partner according to the present invention may solve the problems concerning a low yield and solubility and folding that conventional fusion partners have, and be widely used for protein drug and industrial protein production.

Abstract: Disclosed is a method of producing a target protein having improved solubility and folding efficiency, characterized by expressing a target protein as a fusion protein using an RNA-binding protein as a fusion partner, and binding the fusion partner fused to the target protein to an RNA molecule. More particularly, the present invention discloses a method of producing a target protein having improved solubility and folding efficiency, comprising constructing an expression vector encoding a fusion protein using a target protein and an RNA-binding protein as a fusion partner of the target protein; constructing an expression vector expressing an RNA molecule capable of binding to the RNA-binding protein; and cotransforming a host cell with the expression vectors and then culturing the resulting transformant, wherein the expressed fusion protein binds to the overexpressed RNA molecule. The method of the present invention is very useful for production of proteins for medical and industrial applications.

Abstract: The subject matter of the invention is directed to a single-chain insulin analog that is used to treat diabetes by gene therapy methods.

Abstract: A process for preparing human insulin, which comprises the steps of: preparing a DNA encoding a human proinsulin derivative having the following formula (I); inserting the DNA into a vector to construct an expression vector for the expression of the human proinsulin derivative; transforming a host cell with the expression vector; culturing the resulting transformant under a condition that allows the expression of the human proinsulin derivative; purifying human proinsulin derivative from the culture; and preparing human insulin from the human proinsulin derivative by an enzymatic hydrolysis:B chain-Z-A chain (I)Wherein,said A and B chains are respectively human insulin chains;Z is a peptide of formula U-U-X-P-J-(X')n-U-U;U is an arginine or lysin residue;X and X' are independently any amino acid residue;P is a proline residue;J is a glycine, arginine or lysine residue; andn is 0 or an integer of 1 to 5.

Abstract: Muteins of human tumor necrosis factor (hTNF), a process for production thereof, and DNAs encoding these muteins are found to have a superior antitumor activity and lower acute lethal toxicity compared to the wild-type human tumor necrosis factor.