Abstract: Disclosed is a method for preparing an immunoglobulin (Ig) concentrate useful for treating RSV infection, including a step consisting in subjecting an Ig composition derived from blood plasma to affinity chromatography utilizing an RSV-specific ligand. In a particular embodiment, the RSV-specific ligand is an RSV F protein, preferentially in prefusion conformation, or a variant or an antigenic fragment thereof.

Abstract: The invention relates to a method for immobilizing nucleic ligands including at least one reactive amine function, by grafting on an activated solid substrate, including a step of coupling said nucleic acids on said activated solid substrate having a pH of less than 6.

Abstract: An affinity substrate for the selective binding of a protein of blood plasma includes a solid substrate material on which are immobilized deoxyribonucleic aptamers specifically binding with the plasma protein.

Abstract: A method for purifying GLA-domain coagulation proteins, includes the following steps: a) bringing a sample containing one or more GLA-domain coagulation proteins into contact with an affinity substrate on which nucleic aptamers which bind specifically to the GLA-domain coagulation proteins are immobilized, in order to form complexes between (i) the nucleic aptamers and (ii) the GLA-domain coagulation protein(s), b) releasing the GLA-domain coagulation protein(s) from the complexes formed in step a), and c) recovering the GLA-domain coagulation protein(s) in a purified form.

Abstract: The invention relates to nucleic acid aptamers binding specifically to factor H, to a method for obtaining same, and to the uses thereof, in particular for the purposes of purifying factor H.

Abstract: The invention relates to a method for purifying or detecting a target protein present in a solution, wherein said method comprises, before carrying out the purification or detection step itself, the step of contacting said solution with an aptamer binding specifically to said target protein, wherein said aptamer does not bind to any protein homologous to said target protein that could also be present in the solution.

Abstract: A method for purifying or detecting a target protein present in a solution, includes, before carrying out the actual detection or purification step, a step of contacting the solution with an aptamer binding specifically to the target protein, where the aptamer does not bind to a protein homologous to the target protein that could also be present in the solution.

Abstract: The invention relates to nucleic acid aptamers binding specifically to factor H, to a method for obtaining same, and to the uses thereof, in particular for the purposes of purifying factor H.

Abstract: A method for measuring immunoglobulin G-mediated complement activation, includes the following steps: a) preparing a sample A of immunoglobulin G and a sample B including natural serum, the natural serum optionally being diluted in a dilution buffer; b) mixing sample A with sample B at a ratio (amount of IgG in A in grams):(volume of natural serum in B in liters) of between and 75, at a temperature of between 2° C. and 6° C., and subsequently incubating the resulting reaction mixture at a temperature of between 35° C. and 40° C. for a period of between 30 minutes and 2 hours; c) cooling the reaction mixture obtained at the end of step b) to a temperature of between 0° C. and 4° C. in the presence of EDTA; and d) measuring the amount of C5a fragment in the cooled reaction mixture obtained in c).

Abstract: The invention relates to a method for immobilizing nucleic ligands including at least one reactive amine function, by grafting on an activated solid substrate, including a step of coupling said nucleic acids on said activated solid substrate having a pH of less than 6.

Abstract: The present invention is directed to an affinity chromatography column comprising the antithrombin III (ATIII) protein bound to a solid support, characterized in that: a. the ATIII protein is the wild-type protein or a variant thereof, b. the ATIII protein has been first activated by incubation with an unmodified low-molecular-weight heparin (LMWH) rich in active species, and c. the ATIII protein is covalently bound to a resin in a ratio of less than approximately 2 mg of protein per ml of hydrated resin. The invention is also directed to the use of the aforesaid column for purifying species having an affinity for ATIII in a sample comprising species having affinity and not having affinity for ATIII.

Abstract: A method for purifying GLA-domain coagulation proteins, includes the following steps: a) bringing a sample containing one or more GLA-domain coagulation proteins into contact with an affinity substrate on which nucleic aptamers which bind specifically to the GLA-domain coagulation proteins are immobilized, in order to form complexes between (i) the nucleic aptamers and (ii) the GLA-domain coagulation protein(s), b) releasing the GLA-domain coagulation protein(s) from the complexes formed in step a), and c) recovering the GLA-domain coagulation protein(s) in a purified form.

Abstract: A method for measuring immunoglobulin G-mediated complement activation, includes the following steps: a) preparing a sample A of immunoglobulin G and a sample B including natural serum, the natural serum optionally being diluted in a dilution buffer; b) mixing sample A with sample B at a ratio (amount of IgG in A in grams):(volume of natural serum in B in liters) of between and 75, at a temperature of between 2° C. and 6° C., and subsequently incubating the resulting reaction mixture at a temperature of between 35° C. and 40° C. for a period of between 30 minutes and 2 hours; c) cooling the reaction mixture obtained at the end of step b) to a temperature of between 0° C. and 4° C. in the presence of EDTA;and d) measuring the amount of C5a fragment in the cooled reaction mixture obtained in c).

Abstract: An affinity substrate for the selective binding of a protein of blood plasma includes a solid substrate material on which are immobilized deoxyribonucleic aptamers specifically binding with the plasma protein.

Abstract: A nucleic acid includes at least 15 nucleotides with a length specifically binding with the human factor VII/VIIa.

Abstract: An affinity substrate for selectively binding a coagulation protein, includes a substrate solid on which nucleic aptamers binding specifically to the coagulation protein are immobilized.

Abstract: A method for purifying or detecting a target protein present in a solution, includes, before carrying out the actual detection or purification step, a step of contacting the solution with an aptamer binding specifically to the target protein, where the aptamer does not bind to a protein homologous to the target protein that could also be present in the solution.

Abstract: The present invention is directed to an affinity chromatography column comprising the antithrombin III (ATIII) protein bound to a solid support, characterized in that: a. the ATIII protein is the wild-type protein or a variant thereof, b. the ATIII protein has been first activated by incubation with an unmodified low-molecular-weight heparin (LMWH) rich in active species, and c. the ATIII protein is covalently bound to a resin in a ratio of less than approximately 2 mg of protein per ml of hydrated resin. The invention is also directed to the use of the aforesaid column for purifying species having an affinity for ATIII in a sample comprising species having affinity and not having affinity for ATIII.