Abstract: The problem to be addressed by the present invention is to provide improved recombinant Fc?RIIb and Fc?RIIa that do not require refolding and exhibit high productivity and thermal stability, and to provide a method for producing the same. Said problem is solved by improved recombinant Fc?RIIb comprising at least the amino acid residues of the extracellular domain of human Fc?RIIb (No. 43 to No. 215 in UniProt No. P31994), wherein, in said amino acid residues, at least one amino acid substitution has occurred at a position corresponding to No. 82, 94, 98, 104, 105, or 139 in UniProt No. P31994. Said problem is also solved by improved recombinant Fc?RIIa comprising at least the amino acid residues of the extracellular domain of human Fc?RIIa (No. 34 to No. 206 in UniProt No. P12318-1), wherein, in said amino acid residues, at least one amino acid substitution has occurred at a position corresponding to No. 73, 85, 89, 95, 96, or 130 in UniProt No. P12318-1.

Abstract: Provided are: an Fc-binding protein having improved stability, particularly to heat and acid; a method for producing the protein; an antibody adsorbent using the protein; and a method for separating the antibodies using the adsorbent. Specifically provided are: an Fc-binding protein having improved stability to heat and acid, achieved by substituting an amino-acid residue in a specific position in the extracellular region of human FcyRIIIa with another specific amino acid; a method for producing the protein; an antibody adsorbent using the protein; and a method for separating the antibodies using the adsorbent.

Abstract: The present invention addresses the first problem of providing an Fc-binding protein having improved stability, especially stability to heat and acid, of the Fc-binding protein, a method for producing this protein, and an antibody adsorbent using this protein. The present invention also addresses the second problem of providing a method that makes it possible to identify the presence or absence of glycosylation of an antibody, and a material to be used in this method. The first problem is solved by an Fc-binding protein having improved stability to heat and acid obtained by substituting amino acid residues at specific positions in the extracellular domain within human Fc?RIIIa with other specific amino acids, a method for producing this protein, and an antibody adsorbent using this protein. The second problem is solved by using an adsorbent capable of specifically adsorbing an antibody having a sugar chain, the adsorbent being obtained by immobilizing human Fc?RIIIa on an insoluble carrier.

Abstract: The problem to be addressed by the present invention is to provide improved recombinant Fc?RIIb and Fc?RIIa that do not require refolding and exhibit high productivity and thermal stability, and to provide a method for producing the same. Said problem is solved by improved recombinant Fc?RIIb comprising at least the amino acid residues of the extracellular domain of human Fc?RIIb (No. 43 to No. 215 in UniProt No. P31994), wherein, in said amino acid residues, at least one amino acid substitution has occurred at a position corresponding to No. 82, 94, 98, 104, 105, or 139 in UniProt No. P31994. Said problem is also solved by improved recombinant Fc?RIIa comprising at least the amino acid residues of the extracellular domain of human Fc?RIIa (No. 34 to No. 206 in UniProt No. P12318-1), wherein, in said amino acid residues, at least one amino acid substitution has occurred at a position corresponding to No. 73, 85, 89, 95, 96, or 130 in UniProt No. P12318-1.

Abstract: Provided are: an Fc-binding protein having improved stability, particularly to heat and acid; a method for producing the protein; an antibody adsorbent using the protein; and a method for separating the antibodies using the adsorbent. Specifically provided are: an Fc-binding protein having improved stability to heat and acid, achieved by substituting an amino-acid residue in a specific position in the extracellular region of human FcyRIIIa with another specific amino acid; a method for producing the protein; an antibody adsorbent using the protein; and a method for separating the antibodies using the adsorbent.

Abstract: Provided are: an Fc-binding protein having improved stability, particularly to heat and acid; a method for producing the protein; an antibody adsorbent using the protein; and a method for separating the antibodies using the adsorbent. Specifically provided are: an Fc-binding protein having improved stability to heat and acid, achieved by substituting an amino-acid residue in a specific position in the extracellular region of human FcyRIIIa with another specific amino acid; a method for producing the protein; an antibody adsorbent using the protein; and a method for separating the antibodies using the adsorbent.

Abstract: Disclosed are: an Fc binding protein having increased stability with respect to heat, acid, and/or alkalinity compared with the wild type; a method for producing same; and a method for specifically isolating protein containing an Fc binding protein binding site using said Fc binding protein as a ligand for affinity chromatography. An Fc binding protein was obtained having increased stability with respect to heat, acid, and/or alkalinity compared with the wild-type human Fc receptor by means of substituting at least one specific amino acid residue in the extracellular domain of the wild-type human Fc receptor with another amino acid residue. The Fc binding protein is useful as a ligand for affinity chromatography for example by immobilizing in a solid phase.

Abstract: The present invention addresses the first problem of providing an Fc-binding protein having improved stability, especially stability to heat and acid, of the Fc-binding protein, a method for producing this protein, and an antibody adsorbent using this protein. The present invention also addresses the second problem of providing a method that makes it possible to identify the presence or absence of glycosylation of an antibody, and a material to be used in this method. The first problem is solved by an Fc-binding protein having improved stability to heat and acid obtained by substituting amino acid residues at specific positions in the extracellular domain within human Fc?RIIIa with other specific amino acids, a method for producing this protein, and an antibody adsorbent using this protein. The second problem is solved by using an adsorbent capable of specifically adsorbing an antibody having a sugar chain, the adsorbent being obtained by immobilizing human Fc?RIIIa on an insoluble carrier.

Abstract: A method for producing a carotenoid comprising the steps of cultivating a cell transformed with a DNA sequence comprising a DNA sequence depicted in anyone of SEQ ID NOs: 2-7 or a cell transformed with a vector having a DNA sequence depicted in anyone of SEQ ID NOs: 2-7 under proper culture conditions and isolating the carotenoid from the cell or the culture.

Abstract: A carotenoid producing bacterium belonging to the genus Paracoccus that selectively produces canthaxanthin so that the amount thereof is not less than 90 percent by weight of the total amount of produced carotenoids including ?-carotene, ?-cryptoxanthin, echinenone, canthaxanthin, 3-hydroxyechinenone, 3?-hydroxyechinenone, zeaxanthin, phoenicoxanthin, adonixanthin, and astaxanthin. A method for producing canthaxanthin by culturing the above bacterium, and then collecting carotenoids from bacterial cells or a culture solution after the culturing.

Abstract: Disclosed is a T7 RNA polymerase mutant having improved thermal stability and/or specific activity in comparison with wild-type T7-like bacteriophage RNA polymerase, wherein at least one amino acid residue corresponding to at least one of the amino acid residues selected from the group at least consisting of glutamine at position 768, lysine at position 179 and valine at position 685 of the amino acid sequence that composes wild-type T7 RNA polymerase shown in SEQ ID NO: 6, is substituted with another amino acid.

Abstract: Disclosed are: an Fc binding protein having increased stability with respect to heat, acid, and/or alkalinity compared with the wild type; a method for producing same; and a method for specifically isolating protein containing an Fc binding protein binding site using said Fc binding protein as a ligand for affinity chromatography. An Fc binding protein was obtained having increased stability with respect to heat, acid, and/or alkalinity compared with the wild-type human Fc receptor by means of substituting at least one specific amino acid residue in the extracellular domain of the wild-type human Fc receptor with another amino acid residue. The Fc binding protein is useful as a ligand for affinity chromatography for example by immobilizing in a solid phase.

Abstract: To provide a microorganism capable of producing a large amount of carotenoids, mainly astaxanthin, and to provide a method of producing carotenoids using the microorganism, a microorganism having improved carotenoid productivity is used, which is obtainable by breeding a carotenoid producing Paracoccus bacteria which is featured by producing 720 mg or more carotenoid per 1 L of culture medium. Also used is a method of producing carotenoids using the bacterium.

Abstract: A carotenoid producing bacterium belonging to the genus Paracoccus that selectively produces canthaxanthin so that the amount thereof is not less than 90 percent by weight of the total amount of produced carotenoids including ?-carotene, ?-cryptoxanthin, echinenone, canthaxanthin, 3-hydroxyechinenone, 3?-hydroxyechinenone, zeaxanthin, phoenicoxanthin, adonixanthin, and astaxanthin. A method for producing canthaxanthin by culturing the above bacterium, and then collecting carotenoids from bacterial cells or a culture solution after the culturing.

Abstract: A carotenoid producing bacterium belonging to the genus Paracoccus that selectively produces canthaxanthin so that the amount thereof is not less than 90 percent by weight of the total amount of produced carotenoids including ?-carotene, ?-cryptoxanthin, echinenone, canthaxanthin, 3-hydroxyechinenone, 3?-hydroxyechinenone, zeaxanthin, phoenicoxanthin, adonixanthin, and astaxanthin. A method for producing canthaxanthin by culturing the above bacterium, and then collecting carotenoids from bacterial cells or a culture solution after the culturing.

Abstract: Disclosed is a T7 RNA polymerase mutant having improved thermal stability and/or specific activity in comparison with wild-type T7-like bacteriophage RNA polymerase, wherein at least one amino acid residue corresponding to at least one of the amino acid residues selected from the group at least consisting of glutamine at position 768, lysine at position 179 and valine at position 685 of the amino acid sequence that composes wild-type T7 RNA polymerase shown in SEQ ID NO: 6, is substituted with another amino acid.

Abstract: The present invention intends to provide an IL-6R.IL-6 fusion protein and the like in which IL-6R and IL-6 are directly linked without a linker. The IL-6 receptor.IL-6 fusion protein of the present invention has a structure in which one amino acid residue constituting IL-6 receptor and one amino acid residue constituting IL-6 are directly bonded.

Abstract: [Object] To provide a canthaxanthin selective producing bacterium being able to easily extract and purify canthaxanthin, which is one of carotenoids, and a method for producing canthaxanthin by a culture method. [Solving Means] A carotenoid producing bacterium belonging to the genus Paracoccus is provided which selectively produces canthaxanthin so that the amount thereof is not less than 90 percent by weight of the total amount of produced carotenoids including ?-carotene, ?-cryptoxanthin, echinenone, canthaxanthin, 3-hydroxyechinenone, 3?-hydroxyechinenone, zeaxanthin, phoenicoxanthin, adonixanthin, and astaxanthin. In addition, a method for producing canthaxanthin is provided which has the steps of culturing the above bacterium, and then collecting carotenoids from bacterial cells or a culture solution after the culturing.

Abstract: The present invention intends to provide an IL-6R.IL-6 fusion protein and the like in which IL-6R and IL-6 are directly linked without a linker. The IL-6 receptor.IL-6 fusion protein of the present invention has a structure in which one amino acid residue constituting IL-6 receptor and one amino acid residue constituting IL-6 are directly bonded.

Abstract: A microorganism is provided which allows carotenoid production in industrial production scale. A method of preparing a carotenoid includes: culturing a cell transformed with a DNA chain having a DNA sequence selected from the group consisting of the following (a) to (f) or a cell transformed with a vector having a DNA sequence selected from the group consisting of the following (a) to (f) in an appropriate culture condition, and isolating carotenoid from the cell or a culture medium: (a) DNA sequence encoding a polypeptide having such an enzymatic activity of Paracoccus sp. Strain MBIC1143 that converts a methylene group at 4 position in ?-ionone ring into a keto group (crtW), described in SEQ ID NO: 2, or a substantially homologous DNA sequence thereof; (b) DNA sequence encoding a polypeptide having such an enzymatic activity of Paracoccus sp.