Abstract: This disclosure relates to methods for isolating antibodies from cell-free culture supernatant.

Abstract: Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprises the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein the steps are conducted on one affinity chromatography system.

Abstract: Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprising the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein said steps are conducted on one affinity chromatography system.

Abstract: Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprising the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein said steps are conducted on one affinity chromatography system.

Abstract: Disclosed is an affinity matrix comprising a solid phase and an affinity ligand comprising peptide bonds coupled to this solid phase, wherein the affinity ligand comprising peptide bond is selected from the following group of ligands: a) peptides comprising the formula X1X2X3X4, wherein X1 to X4 are amino acid residues and at least two of X1 to X4 is W, Y or F; b) peptides comprising the formula X5X6X7X8, wherein X5 to X8 are amino acid residues, at least one of X5 to X8 is W, and at least one of X5 to X8 is E or D; and c) poly-amino acids consisting of an amino acid monomer of the group consisting of R, K, E and D and an amino acid monomer of the group consisting of Y, F and W, preferably poly-KY, poly-KF, poly-KW, poly-RY, poly-RF, poly-RW, poly-EY, poly-DY, poly-EF, poly-EW, poly-DF and poly-DW, with the proviso that the peptides according to a) and b) have a maximum length of 35 amino acid residues and that the poly-amino acids according to c) have a minimum length of 20 amino acid residues.

Abstract: The present invention relates to a vector library comprising a multiplicity of different eukaryotic secretion vectors, wherein each vector comprises under the control of transcriptional and translational control sequences a gene encoding for an extracellular soluble fusion polypeptide which gene comprises a coding sequence for a scaffold polypeptide linked to variable coding sequences for a peptide, wherein said vectors comprise a nucleic acid coding for a secretory signal sequence linked to the gene coding for the fusion polypeptide.

Abstract: Disclosed is an affinity matrix comprising a solid phase and an affinity ligand comprising peptide bonds coupled to this solid phase, wherein the affinity ligand comprising peptide bond is selected from the following group of ligands: a) peptides comprising the formula X1X2X3X4, wherein X1 to X4 are amino acid residues and at least two of X1 to X4 is W, Y or F; b) peptides comprising the formula X5X6X7X8, wherein X5 to X8 are amino acid residues, at least one of X5 to X8 is W, and at least one of X5 to X8 is E or D; and c) poly-amino acids consisting of an amino acid monomer of the group consisting of R, K, E and D and an amino acid monomer of the group consisting of Y, F and W, preferably poly-KY, poly-KF, poly-KW, poly-RY, poly-RF, poly-RW, poly-EY, poly-DY, poly-EF, poly-EW, poly-DF and poly-DW, with the proviso that the peptides according to a) and b) have a maximum length of 35 amino acid residues and that the poly-amino acids according to c) have a minimum length of 20 amino acid residues.

Abstract: Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprising the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein said steps are conducted on one affinity chromatography system.

Abstract: The present invention provides a medicament comprising a chemical compound according to formula A: wherein R1 is hydrogen, fluorine, chlorine, bromine, hydroxy, mercapto, methoxy, ethoxy, acetoxy, methyl, ethyl, propyl, isopropyl, t-butyl, nitro, amin, N,N-dimethylaminoyl, N,N-diethyl-aminoyl; R2 is hydrogen, a C1-8-alkyl e.g. methyl, ethyl, propyl, isopropyl, butyl, t-butyl; an C1-8-acyl e.g. acetyl, propionyl; R3 is a C5-12-heterocyclic ring, e.g. furanyl, pyranyl, pyrrolyl, pyridinyl, pyrazolyl, thienyl, thiazolyl, indolyl or -0R4 ; R4 is a C5-C12-aromatic ring e.g. phenyl; unsubstituted or substituted in any position with fluorine, chlorine, bromine, methoxy, ethoxy, C1-8-carboxy; Z is OH or 0; and n is 0, 1, 2 or 3, and m is 0, 1, 2 or 3, and its use for the activation of the aryl hydro carbon receptor.

Abstract: The present invention provides methods for increasing peroxisome proliferator-activated receptor-gamma (PPAR?) activity and/or endothelial nitric oxide synthase (eNOS) activity in a subject by administering to the subject a plant extract or plant juice from thyme, oregano, clove, nutmeg, red clover, bay leaves, red onion or grapes.

Abstract: The invention relates to a method for the selection of epitopes for immunotherapy, peptides obtained by said method, the use of said peptides as vaccines and diagnostics and an immune serum obtainable by said method.

Abstract: In a method for reconstituting a recombinant protein from a denatured state to its active form, a feed solution containing the recombinant protein in its denatured and/or in biologically inactive intermediate forms is subjected to a chromatographic separation process, in which the protein is reconstituted under conditions that promote refolding of the protein and the intermediate forms are separated from the refolded protein. The denatured form and/or the inactive intermediate forms of the protein are separated from the refolded protein in a continuous or quasi-continuous manner and optionally recycled to the feed solution.

Abstract: A process of manufacturing of a chromatography material comprising the steps of (i) reacting a polymerizable at least bifunctional monomer A with a ligand also having a functional group which binds covalently with one of the functional groups of said polymerizable bifunctional monomer A, (ii) to form a compound B comprising at least one polymerizable functional moiety (iii) polymerizing the compound B essentially alone or with the polymerizable monomers in presence of porogenes to obtain a block of porous polymerizate which is self-supporting or (iv) reacting the ligand and a spacer via a covalent bond which is cleavable to form a ligand-spacer conjugate and binding the ligand-spacer conjugate to the surface of a chromatographic support or reacting the ligand-spacer conjugate via a covalent bond to the at least bi-functional monomer A and polymerizing it essentially alone or with the polymerizable monomers in presence of porogenes to obtain a block of porous polymerizate which is self-supporting.

Abstract: A process of manufacturing of a chromatography material comprising the steps of

Abstract: In a method for reconstituting a recombinant protein from a denatured state to its active form, a feed solution containing the recombinant protein in its denatured and/or in biologically inactive intermediate forms is subjected to a chromatographic separation process, in which the protein is reconstituted under conditions that promote refolding of the protein and the intermediate forms are separated from the refolded protein. The denatured form and/or the inactive intermediate forms of the protein are separated from the refolded protein in a continuous or quasi-continuous manner and optionally recycled to the feed solution.

Abstract: Novel human monoclonal anti-HIV-I antibodies and immunochemicals made from the antibodies and method of treating or preventing HIV-I infections.

Abstract: The invention is directed to human monoclonal antibodies specific for the gp41 envelope protein of human immunodeficiency virus type 1 (HIV-1). Specifically disclosed are the human monoclonal antibodies produced by the cell lines 3D6 having ECACC Accession No. 87110301, 24G3 having ECACC Accession No. 90091702 and 25C2 having ECACC Accession No. 80120601.

Abstract: A method for sterilizing liquid chromatography resins that are highly resistant to oxidation by strongly oxidizing agents and a sterilization solution for use therein. In a preferred embodiment, the invention comprises contacting an oxidant-resistant chromatographic resin with an aqueous solution of peracetic acid and up to 40% ethanol. In particular, where the solution is to be used to sterilize a positively charged ion-exchange resin, the solution preferably additionally includes an acetate buffer of a sufficient ionic strength to prevent adsorption of the peracetic acid ions on the resin.

Abstract: A liquid chromatography column well-suited for in situ sterilization effected by washing with a sterilization solution. In a preferred embodiment, the column comprises a liquid chromatography tube packed with a liquid chromatography resin. A piston assembly is mounted within the liquid chromatography tube towards the upper end thereof, the piston assembly including an upper portion and a lower portion, the lower portion being shaped to include a fluid distribution channel and a downwardly-extending collar, the downwardly-extending collar including an annular slot and defining an orifice in fluid communication with the fluid distribution channel.