Abstract: A method of purifying a Growth Factor Protein in a purification sequence employing chromatography is provided. The method comprises performing at least one chromatography step using a multimodal resin, binding the Growth Factor Protein to the multimodal resin at a pH from 4 to 6.2, and eluting the Growth Factor Protein at a pH in the range of from 5.5 to 6.5. The elution of Growth Factor Protein is improved by addition of arginine and/or NaCl in the eluting buffer. Optionally the multimodal resin step is followed by a yeast derived affinity ligand resin step, which results in a purity of the product greater than 90%.

Abstract: A process of purifying a Growth Factor Protein in a purification sequence employing chromatography characterized in that at least one chromatography is performed using a multimodal resin the Growth Factor Protein binds to the multimodal resin at a pH between 4 to 6.2, and the Growth Factor Protein is eluting at a pH >6.3, and the elution of Growth Factor Protein is improved by addition of arginine and/or NaCl to the eluting buffer. The multimodal resin step is followed by a yeast derived affinity ligand resin step, which results of a purity of the product >90%.

Abstract: A process of purifying the Growth Factor Protein G-CSF (Granulocyte Colony Stimulating Factor) in a purification sequence employing chromatography, comprising binding the G-CSF to Capto MMC™, which is a multimodal resin that comprises a negatively charged 2-(benzoylamino) butanoic acid ligand, at a pH from 4 to 6.2; and eluting the G-CSF at a pH greater than 6.3.

Abstract: A process for isolation and purification of a target protein by chromatography wherein the chromatography removes or depletes prions (PrPSc), comprising the steps of contacting a potentially PrPSC-contaminated sample comprising a target protein with a multimodal chromatographic material; setting buffer conditions so that the target protein is bound to the multimodal chromatographic material and whereas PrPSC is not binding to the multimodal chromatographic material; followed by elution of the target protein.

Abstract: A process for isolation and purification of a target protein by chromatography wherein the chromatography removes or depletes prions (PrPSC), comprising the steps of contacting a potentially PrPSC contaminated sample comprising a target protein with a multimodal chromatographic material; setting buffer conditions so that the target protein is bound to the multimodal chromatographic material and whereas PrPSC is not binding to the multimodal chromatographic material; followed by elution of the target protein. a process for isolation and purification of a target protein free of prion protein (prpSC).

Abstract: A process of purifying a Growth Factor Protein in a purification sequence employing chromatography characterized in that at least one chromatography is performed using a multimodal resin the Growth Factor Protein binds to the multimodal resin at a pH between 4 to 6.2, and the Growth Factor Protein is eluting at a pH>6.3, and the elution of Growth Factor Protein is improved by addition of arginine and/or NaCl to the eluting buffer. The multimodal resin step is followed by a yeast derived affinity ligand resin step, which results of a purity of the product>90%.

Abstract: A process of manufacturing a prion-free Vitamin K dependent Protein in a purification sequence employing chromatography characterized in that at least one chromatography step is performed using a multimodal resin providing a fraction containing Vitamin K dependent Protein in an aqueous solution; contacting the fraction containing the Vitamin K dependent Protein with a multimodal resin at a pH between 6-9; optionally washing the multimodal resin having the Vitamin K dependent Protein adsorbed with an aqueous washing buffer to wash away contaminants and retain the Vitamin K dependent Protein, before the Vitamin K dependent Protein is eluted; the Vitamin K dependent Protein is eluting from the multimodal resin at a pH between 6 to 9 in a buffer comprising arginine; and optionally collecting Vitamin K dependent Protein containing fractions in purified or enriched form.

Abstract: A process of purifying or enriching coagulation FVIII employing chromatography comprising the steps of providing a fraction containing FVIII in an aqueous solution having a high ionic strength; contacting the fraction containing FVIII with a multimodal resin; optionally washing the multimodal resin having FVIII adsorbed with an aqueous washing buffer; eluting FVIII containing fractions by an aqueous elution buffer comprising at least one amino acid which is positively charged at pH 6 to 8; and optionally collecting FVIII containing fractions in purified or enriched form.

Abstract: A process of purifying or enriching coagulation FVIII employing chromatography comprising the steps of providing a fraction containing FVIII in an aqueous solution having a high ionic strength; contacting the fraction containing FVIII with a multimodal resin; optionally washing the multimodal resin having FVIII adsorbed with an aqueous washing buffer; eluting FVIII containing fractions by an aqueous elution buffer comprising at least one amino acid which is positively charged at pH 6 to 8; and optionally collecting FVIII containing fractions in purified or enriched form.

Abstract: A process for isolation and purification of a target protein by chromatography wherein the chromatography removes or depletes prions (PrPSC), comprising the steps of contacting a potentially PrPSC contaminated sample comprising a target protein with a multimodal chromatographic material; setting buffer conditions so that the target protein is bound to the multimodal chromatographic material and whereas PrPSC is not binding to the multimodal chromatographic material; followed by elution of the target protein. a process for isolation and purification of a target protein free of prion protein (prpSC).