The present invention is related to a method for identifying a parvovirus mutated structural protein capable of specifically binding to a binder for an antigen, a parvovirus mutated structural protein which comprises at least one B-cell epitope heterologous to the parvovirus, a multimeric structure comprising the protein, a nucleic acid encoding the protein, a virus or cell comprising the protein, a method of preparing the protein, a medicament comprising the protein, nucleic acid or multimeric structure and its use.

The present inventions provide methods for detecting and determining protein structures and stability, including heteromeric protein complexes, in biological fluids, such as serum and other bodily fluids. Systems for performing the methods also are provided.

The present inventions provide methods for detecting and evaluating viruses and virus-like particles using A4F combined with Multi-Angle Light Scattering (MALS) and fluorescent (Flr) detectors. Systems for performing the methods also are provided.

The present invention relates to a method of quantifying the amount of Mock Virus Particles (MVP) removed from a solution as a result of processing that solution through a purification technique. This method involves the steps of adding MVP to a solution, processing the solution through a purification technique, quantifying the amount of MVP removed from the solution. The present invention also relates to a kit that can be used in conjunction with the method. This kit will comprise at least one stock solution of MVP and at least one quantification solution.

Compositions and methods are provided for inhibiting T cell mediated destruction of virally transduced, trangene containing cells.

The present invention relates to a method for the detection of the capsid titer of an adeno-associated virus (AAV) and to a method for the determination of the ratio of full and empty capsids of an AAV by the use of an affinity matrix.

The present invention provides methods for detecting viral infectivity and content in an enzyme preparation. In certain embodiments, the invention relates to methods for producing a pharmaceutical pancreatic enzyme composition. In additional embodiments, the invention relates to detecting infectious porcine parvovirus (PPV) and determining PPV content in pancreatic enzyme preparations (PEPs), including pancrelipase preparations.

Disclosed is a novel means of simultaneously detecting a human parvovirus B19 antigen and an IgM type anti-human parvovirus B19 antibody. The method of simultaneously detecting a human parvovirus B19 antigen and an IgM type anti-human parvovirus B19 antibody in a sample according to the present invention comprises bringing a sample into contact with (1) a 1st probe for detecting the parvovirus B19 antigen and (2) a 2nd probe for detecting the IgM type anti-parvovirus B19 antibody in the presence of a surfactant within the same reaction.

The present invention provides methods for detecting viral infectivity and content in an enzyme preparation. In certain embodiments, the invention relates to methods for producing a pharmaceutical pancreatic enzyme composition. In additional embodiments, the invention relates to detecting infectious porcine parvovirus (PPV) and determining PPV content in pancreatic enzyme preparations (PEPs), including pancrelipase preparations.

The present invention provides: a recombinant expression vector comprising a gene encoding a porcine parvovirus VP2 protein; a recombinant plant or a recombinant insect cell transformed with the vector; and a vaccine composition for a porcine parvovirus and a composition for diagnosing porcine parvovirus, both of which contain a porcine parvovirus VP2 protein obtained from the recombinant plant or the recombinant insect cell. When the recombinant plant or recombinant insect cell of the present invention is used, the porcine parvovirus antigenic protein can be produced with high efficiency, and the porcine parvovirus antigenic protein production method using the recombinant plant or recombinant insect cell has excellent safety and stability compared with other antigen production methods.