The present disclosure provides devices, systems, kits and methods useful for quantitation of biomolecules such as intact proteins and nucleic acids.

By using a graft polymer comprising a dendritic polymer with a styrene skeleton and a hydrophilic polymer grafted to a terminal thereof, a temperature-responsive substrate for cell culture having a temperature-responsive surface for cell culture that allows cells to be cultured with high efficiency and which yet allows cultured cells to be exfoliated in a short period of time and with high efficiency by simply changing the temperature of the substrate surface can be prepared conveniently. If this temperature-responsive substrate for cell culture is used, cells obtained from a variety of tissues can be cultured with high efficiency. If this culture method is utilized, cultured cells can be exfoliated intact in a short amount of time with high efficiency. In addition, by using this graft polymer, a wide range of peptides and proteins can also be separated by simply changing the temperature of a chromatographic carrier. This allows for convenient separation procedure and improves the efficiency of separating operations. What is more, the stereoregularity of the dendritic polymer per se may be utilized to enable separation of solutes based on differences in their molecular structures.

Solutions, detection methods and chromatographic systems are provided for electrospray ionization of glycans modified with amphipathic, strongly basic moieties. The solutions for use in electrospray ionization comprise a plurality of glycans having an amphipathic moiety, a basic residue of pKa>5 and a Log P value between 1 and 3, and one or more volatile components selected from the group consisting of an amine, ammonia, ammonia salt, diethylamine, or trimethylamine. The solutions also have a pH between about 3 to about 6, and ionic strength of between about 0 mM to about 500 mM. The solutions are useful in detecting modified glycans in electrospray ionization and in various chromatographic systems.

This invention relates to a hybrid ligand, a hybrid biomimetic chromedia and a preparing method and a use thereof, wherein the hybrid biomimetic chromedia takes hydrophilic porous microsphere as a substrate in chromatography, activated with allyl bromide and undergoing bromo-alcoholization with N-bromosuccinimide, then coupled with the hybrid ligands. The sequence of the hybrid ligand is phenylalanine-tyrosine-glutamine-5-aminobenzimidazole. The hybrid biomimetic chromedia has both of the two functional groups of phenylalanine-tyrosine-glutamine tripeptide and aminobenzimidazole, while maintaining the high antibody selectivity of polypeptide ligand, hydrophobic electric charge inductive ligand is introduced to achieve more moderate elution requirement, realizing effective antibody separation.

The present invention provides a process for preparing a functionalised polymeric chromatography medium, which process comprises (I) providing two or more non-woven sheets stacked one on top of the other, each said sheet comprising one or more polymer nanofibres, (II) simultaneously heating and pressing the stack of sheets to fuse points of contact between the nanofibres of adjacent sheets, and (III) contacting the pressed and heated product with a reagent which functionalises the product of step (II) as a chromatography medium.

The present disclosure relates to, inter alia, a method of quantitating an amount of an antibody molecule from a mixture comprising two or more antibody molecules, comprising separating each of the two or more antibody molecules from the mixture by hydrophobic interaction chromatography high performance liquid chromatography (HIC-HPLC) and quantitating an amount of each antibody molecule, wherein the molecular weight of each antibody molecule is within 15 kDa of any other antibody molecule in the mixture and either each antibody molecule is different from another antibody molecule in the mixture by more than about 0.25 unit on the Kyte & Doolittle hydropathy scale or each of the antibody molecules when nm alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

The invention relates to a method for controlling preparative liquid chromatography, comprising the following steps, at least a part of said steps being implemented by a computer comprising a processor and a display screen coupled to said processor: (a) selecting an analytical liquid chromatography method from among thin layer chromatography (TLC) and high performance liquid chromatography (HPLC), (b) inputting analytical liquid chromatography data obtained by the method selected at step (a) for a product to be purified, (c) accessing a table of separating tools available to the user to implement said preparative liquid chromatography, (d) from said analytical liquid chromatography data and table of available separating tools, selecting an optimal separating tool from said table and computing preparative liquid chromatography operating conditions for said selected separating tool.

The present invention provides novel chromatographic materials, e.g., for chromatographic separations, processes for its preparation and separations devices containing the chromatographic material; separations devices, chromatographic columns and kits comprising the same; and methods for the preparation thereof. The chromatographic materials of the invention are high purity chromatographic materials comprising a chromatographic surface wherein the chromatographic surface comprises a hydrophobic surface group and one or more ionizable modifier.

Purification methods suitable for purification of bacterial capsular polysaccharides from Streptococcus strains are provided.

The present invention describes a simple purification process for recombinant human serum albumin. The process results in highly purified protein with limited number of purification steps. The broth containing human albumin is clarified by centrifugation and microfiltration, diafiltered and captured by cation exchange chromatography by a process that allows 140-230 mg of albumin to be captured per ml of resin. Product related impurities are removed by hydrophobic interaction chromatography, optimised to allow 87-97% recovery in flow through mode. The final series of processes are so combined that there is easy transition from one step to the next with minimal interventions and adjustments. The entire process of purification is completed within two days from harvest to final product. Thus a cost-effective process with improved recovery of protein at each step is developed. The purified human serum albumin is analyzed for purity and shows physicochemical characteristics that are similar to standard albumin.