Abstract: An object of the present invention is to create a novel engineered Protein A ligand having better antibody dissociation properties in the acidic condition compared with known engineered Protein A ligands. The present invention provides a protein having an affinity for an immunoglobulin, including an amino acid sequence obtained by introducing, into an amino acid sequence derived from any of E, D, A, B and C domains of Protein A, at least one amino acid substitution at any one or more of amino acid residues corresponding to positions 31 to 37 of the A, B and C domains (positions 29 to 35 of the E domain, positions 34 to 40 of the D domain), which are conserved in all the domains, the protein having a lower affinity for an Fab region of an immunoglobulin than a protein having the amino acid sequence before introduction of the substitution.

Abstract: A method for producing a protein includes adsorbing a protein including a ? chain variable region on an insoluble carrier of an affinity separation matrix by contacting a liquid sample including the protein with the affinity separation matrix; washing the affinity separation matrix to remove impurities; separating the protein from the affinity separation matrix by using an acidic buffer; and regenerating the affinity separation matrix by using an alkaline aqueous solution after the protein is separated from the affinity separation matrix. The insoluble carrier includes a ligand immobilized on the insoluble carrier, and the ligand is a ? chain variable region-binding peptide including B5 domain of Protein L derived from Peptostreptococcus magnus 312 strain or a variant of the B5 domain. The adsorbing, the washing, and the separating are repeated 3 or more times.

Abstract: A first immunoglobulin ? chain variable region-binding peptide includes an amino acid sequence of SEQ ID NO: 20 with at least one substitution at one or more positions selected from the group consisting of the 41st position and the 42nd position. A second immunoglobulin ? chain variable region-binding peptide includes the amino acid sequence further comprising 1 to 20 amino acid deletions, substitutions and/or additions at one or more positions except for the 41st position and the 42nd position. A third immunoglobulin ? chain variable region-binding peptide includes an amino acid sequence having a sequence identity of 80% or more with the amino acid sequence of the first peptide, provided that the at least one substitution is not further mutated. The second and third peptides have a higher chemical stability to an alkaline aqueous solution than the chemical stability of the first peptide before introducing the substitution.

Abstract: The present technology relates to a solid-state imaging element configured so that pixels can be more reliably separated, a method for manufacturing the solid-state imaging element, and an electronic apparatus. The solid-state imaging element includes a photoelectric converter, a first separator, and a second separator. The photoelectric converter is configured to perform photoelectric conversion of incident light. The first separator configured to separate the photoelectric converter is formed in a first trench formed from a first surface side. The second separator configured to separate the photoelectric converter is formed in a second trench formed from a second surface side facing a first surface. The present technology is applicable to an individual imaging element mounted on, e.g., a camera and configured to acquire an image of an object.

Abstract: This light-receiving element includes a plurality of photoelectric conversion layers, each of which includes a compound semiconductor, and absorbs a wavelength in an infrared region to generate an electric charge, and an insulating film that is provided to surround each of the plurality of photoelectric conversion layers.

Abstract: This light-receiving element includes: a substrate; a photoelectric conversion layer that is provided on the substrate and includes a first compound semiconductor, and absorbs a wavelength in an infrared region to generate electric charges; a semiconductor layer that is provided on the photoelectric conversion layer and includes a second compound semiconductor, and has an opening in a selective region; and an electrode that buries the opening of the semiconductor layer and is electrically coupled to the photoelectric conversion layer.

Abstract: An object of the present invention is to provide a technique to create novel engineered protein ligands that, when immobilized through a lysine residue (its side chain ?-amino group) which allows for efficient immobilization to a carrier, show the optimum binding capacity and binding efficiency to a target molecule. The present invention provides an engineered protein having a sequence obtained by replacing all the lysine residues in Protein A, which is the most typical protein ligand, with other amino acids, and adding lysine at a terminal; and an affinity separation matrix in which such an engineered protein is immobilized on a water-insoluble carrier by reductive amination or the like. This affinity separation matrix is characterized by its high binding capacity to a target molecule even when the immobilized amount of the ligand is small.

Abstract: A protein includes an amino acid sequence derived from a sequence selected from the group consisting of SEQ ID NOs: 1 to 5. The amino acid sequence includes a substitution of a hydrophobic amino acid residue in an Fc binding site with a different hydrophobic amino acid residue or a polar uncharged amino acid residue, and the protein has a reduced antibody-binding capacity in an acidic pH range, as compared to a protein including the amino acid sequence without the substitution.

Abstract: A protein includes an amino acid sequence derived from a sequence selected from the group consisting of SEQ ID NOs: 1 to 5. The amino acid sequence includes a substitution of a hydrophobic amino acid residue, an acidic amino acid residue, or a polar uncharged amino acid residue with a basic amino acid residue, and the protein has a reduced antibody-binding capacity in an acidic pH range, as compared to a protein including the amino acid sequence without the substitution.

Abstract: A protein includes an amino acid sequence derived from the sequence of SEQ ID NO: 1, wherein the amino acid sequence includes a substitution of Val at a position corresponding to position 40 of SEQ ID NO: 1 with a polar uncharged amino acid residue, a basic amino acid residue, or Ala. The protein has a reduced antibody-binding capacity in an acidic pH range, as compared to a protein including the amino acid sequence without the substitution.

Abstract: A method for purifying an antibody-like protein includes adsorbing an antibody-like protein onto an affinity separation matrix by bringing the antibody-like protein into contact with the affinity separation matrix; and eluting the antibody-like protein by bringing an eluent having a pH of 3.5 or higher into contact with the affinity separation matrix. The affinity separation matrix includes a carrier and a ligand immobilized on the carrier, and the ligand includes an amino acid sequence derived from a sequence selected from the group consisting of SEQ ID Nos: 1 to 5. Gln or Lys in an Fc-binding site of the amino acid sequence is substituted by Ala, Ser, or Thr, and the ligand has a lower antibody-binding capacity in an acidic pH range, as compared to a ligand including the amino acid sequence without the substitution.

Abstract: A protein includes two or more amino acid sequences, wherein each amino acid sequence is derived from a sequence selected from the group consisting of SEQ ID NOs:1 to 5. The amino acid sequence closest to the N-terminus includes a substitution of an amino acid residue at a position corresponding to position 4 or 7 of SEQ ID NO: 5 with an amino acid residue other than Arg, and productivity of the protein in a transformant producing the protein is improved, as compared to productivity of a protein including the amino acid sequence without the substitution.

Abstract: An object of the present invention is to develop techniques to create novel engineered protein ligands that maximize the binding capacity and binding efficiency to a target molecule of affinity separation matrices on which the protein ligands are immobilized. The present invention provides protein ligands (variants) that can be immobilized on carriers in a manner shown in schematic FIG. 1(4)-(15), as well as antibody affinity separation matrices obtained by immobilizing such a protein ligand on a water-insoluble carrier. The affinity separation matrices are characterized by their excellent binding capacity and binding efficiency to a target molecule.

Abstract: The objective of the present invention is to provide a peptide of which both of binding forces to a Fc region and a Fab region are superior. In addition, the objective of the present invention is to provide a DNA which encodes the peptide, a vector which contains the DNA, and a transformant which is transformed by the vector. The problem can be solved by providing the peptide having the specific sequence.

Abstract: A first immunoglobulin ? chain variable region-binding peptide includes an amino acid sequence of SEQ ID NO: 21 with substitution of one or more amino acid residues at the 15th position, the 16th position, the 17th position or the 18th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second immunoglobulin ? chain variable region-binding peptide further includes deletion, substitution and/or addition of 1-20 amino acid residues at positions other than the 15th position, the 16th position, the 17th position and the 18th position. A third immunoglobulin ? chain variable region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first immunoglobulin ? chain variable region-binding peptide.

Abstract: A first Fab region-binding peptide includes an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5 with substitution of one or more amino acid residues at the 17th position and the 36th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second Fab region-binding peptide further includes deletion, substitution and/or addition of one or more amino acid residues at positions other than the 17th position and the 36th position. A third Fab region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first Fab region-binding peptide.

Abstract: The objective of the present invention is to provide an affinity separation matrix having excellent adsorption performance and binding capacity to a peptide containing a Fab region of IgG, and a method for producing a Fab region-containing peptide using the affinity separation matrix. The affinity separation matrix according to the present invention is characterized in that a Fab region-binding peptide is immobilized as a ligand on a water-insoluble carrier in a density of 1.0 mg/mL-gel or more.

Abstract: An affinity separation matrix includes a water-insoluble base material; and a ligand that is immobilized on the water-insoluble base material, wherein the ligand is an antibody ? chain variable region-binding peptide comprising B5 domain of Protein L derived from Peptostreptococcus magnus 312 strain or a part thereof.

Abstract: The objective of the present invention is to provide a Fab region-binding peptide which is excellent in a binding capability to a Fab region of IgG, an affinity separation matrix which has the peptide as a ligand, and a method for producing a Fab region-containing protein by using the affinity separation matrix. In addition, the objective of the present invention is to provide a DNA which encodes the peptide, a vector which contains the DNA, and a transformant which is transformed by the vector. The above-described problems can be solved by utilizing a Protein G variant having the mutation of an amino acid substitution at the specific position.

Abstract: Live cells of a microorganism in a test sample are detected by the following steps: a) the step of treating the test sample with a topoisomerase poison and/or a DNA gyrase poison, b) the step of extracting DNA from the test sample, and amplifying a target region of the extracted DNA by PCR, and c) the step of analyzing an amplification product.