Abstract: The current invention reports a method for purifying an immunoglobulin, wherein the method comprises applying an aqueous, buffered solution comprising an immunoglobulin in monomeric, in aggregated, and in fragmented form to an anion exchange chromatography material under conditions whereby the immunoglobulin in monomeric form does not bind to the anion exchange material, and recovering the immunoglobulin in monomeric form in the flow-through from the anion exchange chromatography material, whereby the buffered aqueous solution has a pH value of from 8.0 to 8.5. In one embodiment the anion exchange chromatography material is a membrane anion exchange chromatography material.

Abstract: Diagnostic tests for characterizing an individual's risk of developing or having a cardiovascular disease. In one embodiment the present diagnostic test comprises determining the level of myeloperoxidase (MPO) activity in a bodily sample obtained from the individual or test subject. In another embodiment, the diagnostic test comprises determining the level of MPO mass in a bodily sample obtained from the test subject. In another embodiment, the diagnostic test comprises determining the level of one or more select MPO-generated oxidation products in a bodily sample obtained from the test subject. The select MPO-generated oxidation products are dityrosine, nitrotyrosine, methionine sulphoxide or an MPO-generated lipid peroxidation products.

Abstract: The present invention provides methods for identifying patients at increased risk of developing an adverse neurological event in response to a cancer treatment. Methods also include modifying the treatment regimen of said patent dependent on the presence or absence of biomarkers in the patient.

Abstract: A method for extracting IgY (?-livetin) from yolk is disclosed, which comprises the following steps: (A) providing a buffer solution, a yolk sample, and an inorganic salt solution; (B) diluting the yolk sample with the buffer solution to obtain a mixture, stirring the mixture for a predetermined time, and performing a centrifugation on the mixture to obtain a supernatant; and (C) adding the inorganic salt solution into the supernatant to salt out IgY, wherein a pH value of the buffer solution is in a range from 4.6 to 5.4, a salt concentration of the buffer solution is in a range from 0.05 M to 0.15 M, and a saturation degree of the inorganic salt solution is in a range from 30% to 60%.

Abstract: The invention provides a previously uncharacterized protein (gamma secretase activating protein or gSAP) that activates ?-secretase to produce ?-amyloid protein (A?). Deposition of A? has been associated with Alzheimer's disease and other pathologies. The invention thus additionally provides, e.g., screening methods and novel research tools, inhibitors of this novel protein, and methods of diagnosis, treatment and control of Alzheimer's disease and other neurodegenerative conditions associated with deposition of A?.

Abstract: Diagnostic tests for characterizing an individual's risk of developing or having a cardiovascular disease. In one embodiment the present diagnostic test comprises determining the level of myeloperoxidase (MPO) activity in a bodily sample obtained from the individual or test subject. In another embodiment, the diagnostic test comprises determining the level of MPO mass in a bodily sample obtained from the test subject. In another embodiment, the diagnostic test comprises determining the level of one or more select MPO-generated oxidation products in a bodily sample obtained from the test subject. The select MPO-generated oxidation products are dityrosine, nitrotyrosine, methionine sulphoxide or an MPO-generated lipid peroxidation products.

Abstract: Diagnostic tests for characterizing an individual's risk of developing or having a cardiovascular disease. In one embodiment the present diagnostic test comprises determining the level of myeloperoxidase (MPO) activity in a bodily sample obtained from the individual or test subject. In another embodiment, the diagnostic test comprises determining the level of MPO mass in a bodily sample obtained from the test subject. In another embodiment, the diagnostic test comprises determining the level of one or more select MPO-generated oxidation products in a bodily sample obtained from the test subject. The select MPO-generated oxidation products are dityrosine, nitrotyrosine, methionine sulphoxide or an MPO-generated lipid peroxidation products.

Abstract: Anti-A? globulomer antibodies, antigen-binding moieties thereof, corresponding hybridomas, nucleic acids, vectors, host cells, methods of producing said antibodies, compositions comprising said antibodies, uses of said antibodies and methods of using said antibodies. The present invention relates to anti-A? globulomer antibodies having a binding affinity to A?(20-42) globulomer that is greater than the binding affinity of the antibody to A?(1-42) globulomer, antigen-binding moieties thereof, hybridomas producing said antibodies, nucleic acids encoding said antibodies, vectors comprising said nucleic acids, host cells comprising said vectors, methods of producing said antibodies, compositions comprising said antibodies, therapeutic and diagnostic uses of said antibodies and corresponding methods relating to Alzheimer's disease and other amyloidoses.

Abstract: Processes for producing and purifying recombinant proteins are disclosed. In particular, the present disclosure provides processes of producing and purifying multi-subunit proteins expressed in yeast or filamentous fungal cells. The production and/or purification of such proteins are monitored for impurities, preferably using lectin binding assays, such that one or more process parameters may be adjusted to maximize the amount of desired recombinant protein and minimize the amount of glycosylated impurities. The processes can also be monitored for other undesired product-associated impurities, such as aggregates and nucleic acids. In exemplary embodiments, the recombinant proteins are multi-subunit proteins, such as antibodies, the host cell is a yeast, such as Pichia pastoris, and the glycosylated impurity is a glycovariant of the desired recombinant polypeptide, such as an N-linked and/or O-linked glycovariant.

Abstract: The present invention provides, among other things, methods and compositions for treating brain conditions. In some embodiments, the methods include administering to a subject suffering from or susceptible to a brain condition an angiotensin (1-7) peptide via either an intravenous or subcutaneous route of administration.

Abstract: This invention demonstrates the formation of a novel polarized membrane lipid raft signaling module in neurons, in response to several diverse neurotoxic stimuli. This polarization occurs well before neurons commit to die, and is an early mechanism in death signaling. The formation of this signaling module is dependent on cholesterol for its formation and provides a mechanistic explanation for the protective effects of cholesterol depleting drugs in several non-neural models of cell death. As such, the formation of the signaling module lends itself as a novel screen for the identification of new drugs and therapeutics which would retard its formation and protect against neuronal injury and death.

Abstract: The object of the invention is a DNA vaccine, method of inducing the immune response, antibodies specifically recognizing the haemagglutinin H5 of an influenza virus and application of the DNA vaccine. According to the invention, one or two-fold immunization of hens with DNA vaccine containing a cDNA encoding the modified H5 haemagglutinin HA protein, i.e. with the deletion of the cleavage site between HA subunits (this provides for greater safety of the vaccines). Moreover, the encoding region of the HA is modified in such a way that protein production in the bird cells should achieve maximal yield. The main modification is codon optimization for the hens and deletion of the site of proteolytic cleavage between subunits HA1 and HA2.

Abstract: A method for treatment of multiple sclerosis (MS) with Campath-1H with significant efficacy and a favorable safety profile is described, which offers an acceptable benefit/risk ratio. Especially described is the use of Campath-1H (alemtuzumab) for the production of a medicament for the treatment of multiple sclerosis (MS), comprising a first treatment cycle followed by at least one further treatment cycle of Campath-1H (alemtuzumab), in which each treatment cycle comprises 1-5 daily doses which are applied on consecutive days, wherein the daily dose is >0 and ?12 mg, and wherein each treatment cycle is separated from the next cycle by at least 1-24 months. Also described are treatment regimens comprising the administration of less than 12 mg/day of Campath-1H for a period of 1-5 consecutive days.

Abstract: Provided herein is a method of detecting the presence of influenza virus in a sample while minimizing false positives due to presence of one or more other pathogens in the sample, the method including measuring the enzymatic activity of neuraminidase (NA) in the sample under one or more differentiating conditions selected from the group consisting of pH, binding to anti-NanA antibody, size exclusion, hemagglutinin (HA) binding, chemical inhibition, and combinations thereof.

Abstract: Disclosed herein are isolated immunogens including variant hepatitis B surface antigens (HBsAgs). In an example, a variant HBsAg includes a HBsAg with one or more transmembrane domains of the HBsAg replaced with a gp41 antigenic insert. The antigenic insert can include an antigenic polypeptide fragment of gp41 including the membrane proximal region of gp41 and a transmembrane membrane region of gp41. The replacement of a membrane spanning domain of HBsAg with a membrane spanning domain of gp41 anchors gp41 into HBsAg in virtually the identical orientation as on HIV virions and correctly orients the nearby MPR on the lipid layer. Thus, the disclosed variant HBsAgs display the neutralization-sensitive MPR in association with a lipid layer, while presenting it at the most immunogenic site on HBsAg. Also disclosed are uses of these variant HBsAgs, and nucleic acids encoding variant HBsAgs, such as to induce an immune response to HIV-1.

Abstract: Methods are provided for the prevention and treatment of seizures and epilepsy. It is shown herein that leukocyte recruitment plays a key role in the pathogenesis of epilepsy. Treatment with an agent that inhibits leukocyte recruitment has therapeutic and preventative effects in blocking recurrent seizures and epilepsy.

Abstract: Suggested is a process for obtaining immunoglobulins, wherein (a) colostral milk from days 0 to 7 is subjected to thermal treatment, skimming the cream, (b) the skimmed milk such obtained is subjected to sterile microfiltration thus producing a first retentate R1 which contains the casein, and a first permeate P1, (c) the first permeate P1 is subjected to ultrafiltration thus producing a second permeate P2 which contains lactose and minerals, and a second retentate R2, in which the immunoglobulins are concentrated.

Abstract: Neural outgrowth in the central nervous system is achieved by administering chondroitinase AC and/or chondroitinase B to degrade chondroitin sulfate proteoglycans that inhibit or contribute to the inhibition of nervous tissue regeneration.

Abstract: The present invention provides a method for conveniently producing a protein formulation in which viruses are inactivated, without impairing the quality of the obtained protein formulation, characterized by including the step of exposing the protein formulation contaminated with the viruses to a 0.1-2M aqueous solution of arginine, an arginine derivative, or a mixture thereof, the aqueous solution being adjusted to pH 3.5 to 5. The present invention also provides a virus inactivation method characterized by including the step of contacting a virus-containing object with a 0.1-2M aqueous solution of arginine, an arginine derivative, or a mixture thereof, the aqueous solution being adjusted to pH 3.5 to 5.

Abstract: The present invention relates to a method for producing a domain antibody in a yeast, wherein the formation of disulfide bridges in the domain antibody is promoted. The method encompasses the addition of oxidizing agents, preferably oxidizing metal ions, preferably one or more selected from Cu2+, Fe2+, Fe3+ and Zn2+.