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Martinsried, Germany

Scholz M.,Leukocare | Luking A.,Protagen
Biotechnology Journal | Year: 2012

The stability of therapeutic antibodies during downstream processing and storage is important for functionality and quality. To determine functional antibody performance, the UNIchip® high-density protein microarray with 384 recombinant antigenic targets was developed; this allows characterization of antibody specificity by generating standardized quantitative binding profiles. In this study, we used UNIchip® to test the efficacy of a novel protein stabilizing and protecting solution (SPS) to preserve the binding specificity and binding strength of a therapeutic anti-TNF-α antibody (Adalimumab; Humira). Our results show that reconstituted SPS-formulated and lyophilized Adalimumab elicits significantly less off-target activity after reconstitution and preserves binding strength even after six weeks of storage at 40°C compared with Adalimumab that underwent the same treatment with the original formulation. By means of UNIchip®, we were able to confirm the protein stabilizing effects of SPS as shown by preserved antibody functionality. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

The 14th Annual World Vaccine Congress was held in Washington DC, March 24-26, 2014 (http://www.terrapinn. com/vaccine2014). More than 400 experts from different regions participated in this scientific event for vaccine professionals from industry, academia, non-profit organizations and government to discuss challenges and successes from all the major vaccine stakeholders. In more than 70 presentations, round tables, and plenary discussions major topics like emerging and re-emerging infectious disease, vaccine production, and innovative technologies were debated. While most contributions focused on specific questions in vaccine research development, some like the one by a representative of the Bill and Melinda Gates Foundation (BMGF) reported about supply chain, logistics topics, and challenges in vaccine implementation. © 2014 Taylor & Francis Group, LLC.

The present invention, inter alia, relates to a closed sterilized container comprising at least one carrier which is a stabilizer; and at least one biomolecule reversibly attached to the carrier, wherein said carrier partially or completely covers the attached biomolecules and wherein said at least one carrier is selected from the group consisting of (poly)peptides such as dipeptides or tripeptides, amino acids, polyalcohols, polyethyleneglycols, ionic liquids, compatible solutes, saponins and a mixture thereof. The invention also relates to methods for producing sterilized containers according to the invention and uses thereof.

Leukocare | Date: 2010-03-31

The present invention relates to the use of a composition comprising (a) at least three different amino acids, (b) at least two different amino acids and a saponin or (c) at least one dipeptide or tripeptide for stabilizing biomolecules immobilized on a solid carrier. The invention furthermore relates to a method for producing stabilized biomolecules, comprising embedding the biomolecules in the composition according to the invention and a method of producing a solid carrier having biomolecules attached thereto. The invention furthermore relates to a solid carrier producible or produced by the method of the invention and a method of diagnosing a disease using the carrier of the invention.

The present invention relates to a method for preventing the unfolding of a (poly)peptide during drying and/or inducing the (re-)folding of a (poly)peptide after drying, comprising the step of embedding the (poly)peptide in an aqueous solution, wherein the solution comprises (i) at least three different amino acids; or (ii) at least one dipeptide or tripeptide; and wherein the solution is free or substantially free of (a) sugar; and (b-i) protein; and/or (b-ii) denaturing compounds; and (c) silanes.

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