Abstract: The present invention relates to a process for purifying C1-esterase inhibitor (C1-Inh), and more in particular a Cl-Inh concentrate.

Abstract: The present invention relates to means and methods for determining neurotoxin activity. Specifically, it relates to a polypeptide having caspase activity comprising a large subunit and a small subunit wherein the caspase further comprises a neurotoxin cleavage site which upon cleavage activates the caspase activity. Also encompassed are polynucleotides encoding the polypeptides as well as vectors or host cells comprising the polynucleotides. The present invention further relates to a method for determining neurotoxin activity in a sample based on the polypeptide of the invention as well as the use of the polypeptide for determining neurotoxin activity in a sample, in general.

Abstract: The present invention relates to means and methods for determining neurotoxin activity. Specifically, it relates to a polypeptide having caspase activity comprising a large subunit and a small subunit wherein the caspase further comprises a neurotoxin cleavage site which upon cleavage activates the caspase activity. Also encompassed are polynucleotides encoding the polypeptides as well as vectors or host cells comprising the polynucleotides. The present invention further relates to a method for determining neurotoxin activity in a sample based on the polypeptide of the invention as well as the use of the polypeptide for determining neurotoxin activity in a sample, in general.

Abstract: The present invention relates to means and methods for determining neurotoxin activity. Specifically, it relates to a polypeptide having caspase activity comprising a large subunit and a small subunit wherein the caspase further comprises a neurotoxin cleavage site which upon cleavage activates the caspase activity. Also encompassed are polynucleotides encoding the polypeptides as well as vectors or host cells comprising the polynucleotides. The present invention further relates to a method for determining neurotoxin activity in a sample based on the polypeptide of the invention as well as the use of the polypeptide for determining neurotoxin activity in a sample, in general.

Abstract: The present invention relates to means and methods for determining neurotoxin activity. Specifically, it relates to a polypeptide having caspase activity comprising a large subunit and a small subunit wherein the caspase further comprises a neurotoxin cleavage site which upon cleavage activates the caspase activity. Also encompassed are polynucleotides encoding the polypeptides as well as vectors or host cells comprising the polynucleotides. The present invention further relates to a method for determining neurotoxin activity in a sample based on the polypeptide of the invention as well as the use of the polypeptide for determining neurotoxin activity in a sample, in general.

Abstract: Method of measuring an effect induced to a muscle tissue by a clostridial neurotoxin, comprising: (a) contacting a muscle tissue or a cell culture with a sample comprising the clostridial neurotoxin; (c) measuring the effect induced to the muscle tissue by the clostridial neurotoxin; wherein step (c) is performed in the absence of the sample.

Abstract: This application includes description of antibodies for specifically detecting prions of human origin and methods for detecting pathogenic prions. In some embodiments, the antibodies bind to an epitope characteristic of a human prion protein which is not found in the prion proteins of other species. In some embodiments, the antibodies are not cross-reactive with cow, Syrian Gold hamster, mouse, or rat prions. The application also includes a conformation-dependent immunoassay method for detecting pathogenic prions in a sample containing a prion (PrP) protein. The PrP protein may be present in a first conformation and a second conformation, such as PrPc and PrPSc in which the two conformations have different binding affinity for the antibody used to detect them.

Abstract: This application includes description of antibodies for specifically detecting prions of human origin and methods for detecting pathogenic prions. In some embodiments, the antibodies bind to an epitope characteristic of a human prion protein which is not found in the prion proteins of other species. In some embodiments, the antibodies are not cross-reactive with cow, Syrian Gold hamster, mouse, or rat prions. The application also includes a conformation-dependent immunoassay method for detecting pathogenic prions in a sample containing a prion (PrP) protein. The PrP protein may be present in a first conformation and a second conformation, such as PrPc and PrPSc in which the two conformations have different binding affinity for the antibody used to detect them.

Abstract: This application includes description of antibodies for specifically detecting prions of human origin and methods for detecting pathogenic prions. In some embodiments, the antibodies bind to an epitope characteristic for a human prion protein which is not found in the prion proteins of other species. In some embodiments, the antibodies are not cross-reactive with cow, Syrian Gold hamster, mouse, or rat prions. The application also includes a conformation-dependent immunoassay method for detecting pathogenic prions in a sample containing a prion (PrP) protein. The PrP protein may be present in a first conformation and a second conformation, such as PrPC and PrPSc in which the two conformations have different binding affinity for the antibody used to detect them.

Abstract: Antibodies for specifically detecting pathogenic prions of human origin, and methods for detecting pathogenic prions, are described. In particular, a conformation-dependent immunoassay method for detecting pathogenic prion proteins in a sample of a body fluid, containing a PrP protein, which contains a first, natural, non-pathological conformation, i.e. PrPc, and a second, pathological conformation, i.e.