This invention provides chromatographic methods for the purification of a cystathionine -Synthase (CBS) protein, particularly truncated variants thereof and compositions and pharmaceutical compositions prepared therefrom.

The invention relates to a method for determining the presence of at least one distinct polypeptide in a biological sample comprising contacting the biological sample with a hydrolyzing agent, wherein the hydrolyzing agent is capable of hydrolyzing the distinct polypeptide in a sequence-specific manner such that at least one distinct peptide having a predetermined peptide measured accurate mass would result if the at least one distinct polypeptide were present in the biological sample, to obtain a hydrolyzed sample; bringing the hydrolyzed sample in contact with a substrate comprising at least one immobilized binding partner, wherein the at least one immobilized binding partner is capable of specifically binding the distinct peptide; removing the hydrolyzed sample from the substrate in a manner such that the distinct peptide would remain bound to the immobilized binding partner; contacting the substrate with an elution solution, wherein the distinct peptide would dissociate from the immobilized binding partner into the elution solution; subjecting a portion of the elution solution to liquid chromatography to segregate a plurality of molecules in the portion of the elution solution to obtain sorted molecules; determining the measured accurate mass of at least one sorted molecule present in the elution solution; and determining the presence of the at least one distinct polypeptide in the biological sample when a measured accurate mass of at least one molecule is substantially equal to the predetermined peptide measured accurate mass.

Separation of materials is achieved using affinity binding and acoustophoretic techniques. A column provided with a fluid mixture of materials for separation and support structures may be used with acoustic waves to block flow of the support structures. The support structures can have an affinity for one or more materials in the fluid mixture. By blocking flow of the support structures, materials bound or adhered to the support structure are also blocked.

This invention provides chromatographic methods for the purification of a cystathionine -Synthase (CBS) protein, particularly truncated variants thereof and compositions and pharmaceutical compositions prepared therefrom.

The isolation and identification of glycosaminoglycans capable of binding to proteins having a heparin-binding domain is disclosed, as well as the use of the glycosaminoglycans isolated in the growth and/or development of tissue.

The present invention relates to the chromatographic isolation of a target cell or another complex biological material, in particular by column chromatography such as affinity chromatography or gel permeation chromatography. The invention employs a receptor binding reagent that binds to a receptor molecule that is located on the surface of a target cell. The invention in general provides novel methods for the traceless isolation of biologic materials such as cells, cell organelles, viruses and the like. The invention also relates to an apparatus for the isolation of cells and other complex biological materials.

The present disclosure provides viral vector manufacturing and purification methods. Particularly, the disclosure provides improved methods for manufacturing lentiviral vector from host cells grown in suspension. More particularly, the disclosure provides improved large-scale lentiviral manufacturing methods comprising growing cells to a suitable number, transfecting with lentiviral packaging plasmids, a transfer plasmid, and a transfection agent; treating with an endonuclease; harvesting and clarifying the suspension culture supernatant; capturing and concentrating the lentiviral vector using affinity chromatography or cation exchange chromatography; filtering the concentrated lentiviral vector; ultrafiltering and diafiltering the lentiviral vector; formulating the lentiviral vector; and sterile filtering the formulated bulk lentiviral vector.

The present disclosure relates, in some aspects, to protein-ligand localized conjugation technology with respect to immobilized functional proteins for affinity enrichment and/or modified proteins for therapeutic applications.

The present disclosure provides, in one aspect, a device and a method for unit sequencing and/or analysis of a molecular sequence comprising attaching the molecular sequence to a plate and controlling the progression of the molecular sequence through a pore of a nanopore chip, wherein the separation distance between the nanopore chip and the scan plate is controlled by a precision mechanical drive, and the molecular sequence is sensed as it progresses through the nanopore.

The invention relates to heparan sulphate GAGs obtained by affinity chromatography using the heparin-binding domain of BMP2. The GAGs were obtained from osteoblast extracellular matrix and from a commercially available heparan sulfate (Celsus HS).