Abstract: A method for purifying a modified major mite allergen obtained by the genetic recombination technique and a purified modified major mite allergen obtained by said method for purification are provided.

Abstract: Various embodiments of the present invention are directed to multi-step systems and methods for target-molecule purification that employ column-chromatography-based and/or membrane-filtration-based polishing steps. In one described embodiment of the present invention, a target-protein-containing eluate having a high residual salt concentration is collected from a first chromatography column prepared with an affinity-chromatography resin, loaded onto a second chromatography column prepared with a cation-exchange resin, and eluted from the second cation-exchange column using a buffer in which a time-dependent pH gradient is established. In another described embodiment of the present invention, a partially purified target-protein-containing eluate is collected from a chromatography column and further purified by passing the target-protein-containing eluate through a salt-tolerant anion exchanger.

Abstract: A method for refolding a protein by mixing a protein solution with a refolding buffer at mixing conditions that approximate ideal mixing. The method can be carried out batch wise, in a fed-batch mode or continuously with on-line solubilization of inclusion bodies.

Abstract: A method for the production of a purified extract of natural allergens comprising the steps of a) extracting a natural source of allergens comprising allergenic proteins to form an extract, b) purifying of said extract to remove non-protein components to form a purified extract c) denaturating said purified extract to form a purified denaturated extract, said purified denaturated extract comprising proteins, wherein the most abundant (w/w) proteins, forming together at least 60% (w/w) of all proteins, are at least two proteins, and all proteins represent at least 60% (w/w) of the dry weight of the purified denaturated extract and a method for the production of a purified extract of natural allergens comprising the steps of a) hydrolysing a denaturated allergen to form an allergen hydrolysate, b) purifying said allergen hydrolysate to remove peptides with a molecular weight above 10,000 Da and below 1,000 Da in order to obtain a purified hydrolysate where 70%, more preferably 80% of the peptides are betwe

Abstract: A displacement chromatography process and displacer compounds used in the process and having the general formula (I): wherein: each group R1, R2, R3, R?1, R?2, and R?3, independently may be selected from alkyl, aryl, and aralkyl, and in which a ring containing one or more quaternary nitrogen may be formed by any one or more of R1 and R2, R1 and R?1, R1 and R4, R4 and R?4, or R4 and R5; each R4, R?4, R5 and R?5 independently may be selected from alkyl, aryl, aralkyl and —(CH2)a—(CHY)b—(CH2)c—N+R1R2R3 An?, wherein R1, R2 and R3 are as defined above; each Y independently may be selected from —H, —OH, —OR6, halo, alkyl, aryl and aralkyl, wherein —R6 may be alkyl or —(CH2)a—(CHOH)b—(CH2)c—N+R1R2R3 An?, wherein R1, R2 and R3 are as defined above; each q and z independently may be any whole number from 0 to about 6, with the proviso that q+z is equal to or less than about 6; each a, b, and c independently may be any whole number from 0 to 2, with the proviso that the sum a+b+c in any fragment is at least 1; a

Abstract: The invention relates to methods for purifying lactoferrin, stabilizing it in solution and improving its activity. In one embodiment of the present invention, it is provided methods for lactoferrin purification employing hydrophobic and/or hydrophilic adsorbent under specific conditions for maintaining or preserving lactoferrin protein stability. It is also provided a process to remove inhibitor of lactoferrin activity.

Abstract: The present invention relates to a method of purifying a protein of interest from its fusion analog, comprising obtaining a protein solution comprising a protein of interest and its fusion analog; adjusting the pH and/or ionic strength of the protein solution with an appropriate buffer for use with a Hydrophobic Charge Induction Chromatography (HCIC) resin, contacting the protein solution and HCIC resin column to allow binding of the protein of interest and its fusion analog, washing the resin and eluting the protein of interest from the resin by a pH gradient; wherein the protein of interest is substantially free of its fusion analog.

Abstract: A system and method for integrating microfluidic components in a microfluidic system enables the microfluidic system to perform a selected microfluidic function. A capping module includes a microfluidic element for performing a microfluidic function. The capping module is stacked on a microfluidic substrate having microfluidic plumbing to incorporate the microfluidic function into the system. The microfluidic element may comprise a matrix having an affinity for selected molecules in a sample. The matrix binds, reacts with and/or retains the selected molecules without affecting other molecules in the sample.

Abstract: The invention relates to a method for extracting a protein from milk, having at least one hydrophobic pocket and a negative charge to the natural pH of milk, that comprises the following steps: a) skimming and delipidation of the milk; b) passing the delipidated and skimmed fraction containing said protein on a chromatographic substrate on which is grafted a ligand having both a hydrophobic characteristic and a ionic characteristic in pH conditions enabling the protein to be retained on said substrate, the pH being higher than 4.6; c) elution of the protein; d) purification of the eluded fraction by removing the milk proteins from said eluded fraction; and e) recovering said protein.

Abstract: The present invention relates to a separation matrix comprised of a support to the surfaces of which polymer chains have been coupled, wherein each polymer chain presents recurring proton-donating groups and at least the surface of the support is substantially hydrophilic. In the most advantageous embodiment, the support is porous cross-linked agarose, the polymers are poly(acrylic acid) and the proton-donating groups are carboxyl groups. The matrix is useful e.g. to remove PEG from pegylated and/or native compounds in a liquid. Accordingly, the invention also encompasses a method, such as a chromatographic method, wherein the separation matrix according to the invention is used, for example as a pre-treatment of a reaction mixture that comprises unreacted PEG, pegylated proteins and native proteins.

Abstract: A pure, water-soluble polypeptide containing one or more monomers of a VP1 protein of a foot-and-mouth disease virus; or a pure, water-insoluble polypeptide comprising two or more monomers of a VP1 protein of a foot-and-mouth disease virus. Also disclosed are a vaccine containing the polypeptide, a method of producing the polypeptide, and a method of inducing an immune response in a subject by administering to the subject an effective amount of the polypeptide.

Abstract: A process is provided for the preparation of albumin from a yeast culture medium which has extremely low levels of or is essentially free of colorants, metal ions, human proteins, host proteins, fragments of albumin, polymers or aggregates of albumin and viruses, and which is essentially non-glycated, relatively high in free thiol and with an intact C-terminus. The process comprises separating the yeast from the culture medium to yield an albumin solution; subjecting the albumin solution to positive mode cation exchange, affinity, and positive mode anion exchange chromatography; and concentrating and formulating the albumin with sodium octanoate and sodium chloride.

Abstract: The present invention discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.

Abstract: This invention relates to the use of mixed mode chromatography for purification of a protein from a mixture containing other materials, including fragmented or aggregated antibodies, host cell proteins, DNA, endotoxin, and/or virus. This invention further relates to the integration of such a method into a multi-step procedure with other fractionation methods for purification of antibodies or other proteins suitable for in vivo applications.

Abstract: The present invention relates to phosphopeptide isolation and enrichment, particularly to a highly selective and specific phosphopeptide enrichment method. The method mentioned in the invention is based on the strong interaction between zirconium phosphonate and phosphopeptide. Zirconium phosphonate is immobilized on the surface of matrix for phosphopeptide enrichment. Zirconium phosphonate could be immobilized on chip surface, it can also be immobilized on chromatographic matrix for isolation and purification of phosphopeptides. The method shows high specificity for phosphopeptides, it can be applied to purify and enrich low abundance phosphopeptide from biological samples.

Abstract: The present invention relates to a process for purifying fibrinogen, which comprises one or more process steps in which one or more contaminating proteins are depleted by negative chromatography and/or negative adsorption using cation exchanger, hydrophobic gel and/or dye gel. In addition, the invention relates to the fibrinogen which is obtained by the process of the invention and which is notable for improved stability, and to the production and use of pharmaceutical preparations comprising this fibrinogen.

Abstract: A method (100) and a system (200) for processing mammalian bodily fluids to isolate target peptides and proteins. The method can include the steps of passing a mammalian bodily fluid through at least one ion exchange column (204). The ion exchange column can include an anionic resin and/or a cationic resin. The ion exchange column can be selected to remove large particles at a first pH level selected to remove such large particles at a maximum fluid pressure of 30 pounds per square inch (psi), for example less than 10 psi. The large particles can be released from the ion exchange column with a rinse solution having a pH selected for releasing the large particles. The pH of the fluid then can be adjusted to be a value less than 5.0, and the fluid can be filtered with a microfilter or ultrafilter (210).

Abstract: The invention provided is a split-free nano-liter flow liquid chromatography system comprising at least a first and a second chromatographic column connected in series, wherein an autosampler is provided and programmed to inject samples and eluent solutions of increasing eluent concentration for gradually eluting analytes from the first column into the second column (without adversely affecting separation in the second column), said solutions segmented from the mobile phase of the liquid chromatography system by air plugs.

Abstract: The invention provides methods of increasing yields of desired conformation of proteins. In particular embodiments, the invention includes contacting preparations of a recombinant protein with a reduction/oxidation coupling reagent for a time sufficient to increase the relative proportion of a desired configurational isomer.

Abstract: The present invention provides for compositions of anti-M-CSF antibodies that are substantially free of endotoxin. Also provided are methods of treating M-CSF-mediated disorders with pharmaceutical formulations of anti-M-CSF antibodies having reduced endotoxin levels, including inflammatory diseases and neoplasia disorders.

Abstract: Methods for producing improved anti-human thymocyte immunoglobulins from specific-pathogen-free animals are provided, without the need for an adsorption step on human tissues and the consequent drawbacks of such a step.

Abstract: The present invention addresses the need to improve the yields of viral vectors when grown in cell culture systems. In particular, it has been demonstrated that for adenovirus, the use of low-medium perfusion rates in an attached cell culture system provides for improved yields. In other embodiments, the inventors have shown that there is improved Ad-p53 production with cells grown in serum-free conditions, and in particular in serum-free suspension culture. Also important to the increase of yields is the use of detergent lysis. Combination of these aspects of the invention permits purification of virus by a single chromatography step that results in purified virus of the same quality as preparations from double CsCl banding using an ultracentrifuge.

Abstract: The present invention is directed to a method for processing a plant-based protein source, the method comprising an acidic extracting solution comprising a reducing agent is useful for extracting and isolating proteins from plant-based protein sources.

Abstract: A method to more quantitatively recover a peak of a protein and associated aggregates, hydrophobic proteins, or hydrophobic peptides which are typically difficult to recover and detect as a peak, using a commercially available gel filtration chromatography column and a mobile phase is described. More specifically, a compound, such as arginine, which may be added to the mobile phase, thereby eliminating the unnecessary interaction that occurs between the proteins, peptides, or aggregates and the column stationary phase, is described.

Abstract: The present invention relates to bacteriophage tail proteins and the derivatives and fragments thereof that are capable of binding endotoxins in the absence of bivalent positive ions, especially Ca2+ or Mg2+. Further, the present invention relates to methods for depleting endotoxins from solutions and samples using the bacteriophage tail proteins according to the present invention and to a detection method for endotoxins.

Abstract: The present invention provides a method for recombinant production, recovery and purification of endostatin protein. This method may be employed for large scale recovery and purification of recombinantly-produced endostatin protein.

Abstract: A polymer carrier to which a prescribed zinc complex group is binding directly or through a spacer, having property to bond, under a certain condition, to an anionic substituent (a phosphate group, for example), showing low solubility to a solvent (preferably insolubility to a solvent) as a whole, and being capable of capturing, separating and purifying easily a substance having an anionic substituent (a phosphate group, for example).

Abstract: The current invention provides a method for directly converting histopathologically processed biological samples, tissues, and cells into a multi-use biomolecule lysate. This method allows for simultaneous extraction, isolation, solublization, and storage of all biomolecules contained within the histopathologically processed biological sample, thereby forming a representative library of said sample. This multi-use biomolecule lysate is dilutable, soluble, capable of being fractionated, and used in any number of subsequent experiments.

Abstract: The present disclosure relates to a system and method for protein separation including: fractionating a mixture of proteins on a reversed-phase superficially porous stationary phase at a temperature of greater than or equal to about 40° C. to recover a protein in from about 70 to 100 weight percent of the mixture of proteins.

Abstract: The present invention provides a rapid and relatively simple process for purification of acidic proteins expressed in tobacco cells. The process comprises three main purification steps: precipitation with polyethyleneimine, column chromatography with a hydrophobic interaction resin, and column chromatography with hydroxyapatite. The process provides pure or essentially pure protein at a very high yield.

Abstract: The present invention relates to a novel method for the isolation or purification of immunoglobulins (a special class of proteins) from a solution containing immunoglobulins, e.g. hybridoma cell culture supernatants, animal plasma or sera, or colostrum. The method includes the use of a minimum of salts, such as lyotropic salts, in the binding process and preferably also the use of small amounts of organic solvents in the elution process. The solid phase matrices, preferably epichlorohydrin activated agarose matricees, are functionalised with mono- or bicyclic aromatic or heteroaromatic ligands (molecular weight: at the most 500 Dalton) which, preferably, comprises an acidic substituent, e.g. a carboxylic acid. The matrices utilised show excellent properties in a “Standard Immunoglobulin Binding Test” and in a “Monoclonal Antibody Array Binding Test” with respect to binding efficiency and purity, and are stable in 1M NaOH.

Abstract: The present invention provides a completely novel molting hormone receptor, which is used for efficiently screening a substance that can be applied to a disinfestant or the like. An insect molting hormone receptor comprising the following polypeptide (a) and polypeptide (b) or (c): (a) a polypeptide having the amino acid sequence shown in SEQ ID NO: 1; (b) a polypeptide having the amino acid sequence shown in SEQ ID NO: 2; and (c) a polypeptide having the amino acid sequence shown in SEQ ID NO: 3.

Abstract: Embodiments of the present invention are directed to articles of manufacture, devices, methods and apparatus for performing liquid chromatography featuring a chromatographic sorbent having one or more pentafluorophenyl groups, wherein said one or more pentafluorophenyl groups are a bonded phase on a sorbent selected from the group comprising silica, organic polymers or hybrid organic silane material and said pentafluorophenyl groups are in a mono-, bi-, and tridentate forms.

Abstract: This invention provides methods and compositions for producing high titer, substantially purified preparations of recombinant adeno-associated virus (AAV) that can be used as vectors for gene delivery. At the onset of vector production, AAV producer cells of this invention typically comprise one or more AAV packaging genes, an AAV vector comprising a heterologous (i.e. non-AAV) transgene of interest, and a helper virus such as an adenovirus. The AAV vector preparations produced are generally replication incompetent but are capable of mediating delivery of a transgene of interest (such as a therapeutic gene) to any of a wide variety of tissues and cells. The AAV vector preparations produced according to this invention are also substantially free of helper virus as well as helper viral and cellular proteins and other contaminants. The invention described herein provides methods of producing rAAV particles by culturing producer cells under conditions, such as temperature and pH, that promote release of virus.

Abstract: An adsorbent of high-mobility-group proteins (HMG protein) which can remove HMG protein in body fluid is disclosed. The adsorbent according to the present invention has a water-insoluble carrier on which (a) substance(s) having (a) hydrogen-bondable functional group(s) and/or (a) hydrophobic functional group(s) is(are) immobilized.

Abstract: Thus, a primary aspect of the present invention relates to a method for the fractionation of a protein-containing mixture wherein the protein-containing mixture is selected from the group consisting of milk, milk derived products, milk derived raw materials, vegetable derived products, vegetable derived extracts, fruit derived products, fruit derived extracts, fish derived products, and fish derived extracts, said method comprising the steps of: a) optionally adjusting the pH of the mixture; b) applying said mixture to an adsorption column comprising an adsorbent, said adsorbent comprises a particle with at least one high density non-porous core, surrounded by a porous material, the adsorbent having a particle density of at least 1.5 g/ml and a mean particle size of at most 150 ?m; c) optionally washing the column; d) eluting at least one protein from the adsorbent.

Abstract: The invention relates to a method for purifying a factor XIII polypeptide from a biological material, the method comprising subjecting the material to sequential chromatography on an anion-exchange matrix and a hydrophobic interaction matrix.

Abstract: Adding enough organic solvent to hydrophobic interactive chromatography elution buffer eliminates the need to also add detergent to the buffer when separating poly-peptides. For example, adding about 50% acetonitrile to detergent-free elution buffer enaibls one to separate full-length human growth hormone from its various truncated forms, to obtain hGH with a purity of >99.5%. This technique is useful to purify polypeptide where detergent to contamination in the resulting polypeptide is undesirable.

Abstract: The present disclosure relates to a system and method for membrane protein separation including: fractionating a membrane sample on a reversed-phase superficially porous stationary phase at a temperature of greater than or equal to about 40° C. to recover a protein greater than about 70 weight percent of the mixture of proteins.

Abstract: The present invention provides a structural characterization platform that can be used to assess the stability of a polyclonal cell line during production, as well as batch-to-batch consistency of the final polyclonal products. The structural characterization platform is based on genetic analyses as well as protein characterization techniques that alone or in combination provide the necessary information to characterize the polyclonal cell line and final products. The collection of different homologous proteins to be analyzed with the platform techniques if for example a recombinant polyclonal antibody or a mixture of monoclonal antibodies.

Abstract: The present invention is directed to the purification and commercialization of therapeutic polypeptides that have. In one aspect of the invention, a method of purifying Interferon ?-1b using size exclusion chromatography is provided. In another aspect of the invention, a method of purifying a polypeptide using size chromatography is provided. A third aspect provides a method of commercializing a polypeptide.

Abstract: The present invention relates to methods and compositions for treatment of microbial infections and for the enhancement of resistance to infection. The invention comprises administration of an effective amount of bacterial lysate compositions for the treatment of pathological conditions of microbial infections. The present invention can also be used to enhance the immune system to prevent infections by the administration of an effective amount of the compositions.

Abstract: The present invention is directed to a novel method of analysis of high molecular weight proteins. More specifically, it is directed to a novel reversed-phase LC/MS method of analysis of high molecular weight proteins including antibodies.

Abstract: The present invention relates to an ion exchange chromatography process for purifying a peptide from a mixture containing the peptide and related impurities, and to an industrial method including such ion exchange chromatography process.

Abstract: The present invention provides a process for dissociating Fc-containing molecules from complexes of Protein A/Fc-containing molecules or mixtures containing Fc-containing molecules and Protein A. The association, e.g., by hydrophobic interactions, between the Fc-containing molecules and Protein A can be reduced or inhibited by raising the pH of dissociation. The pH of dissociation can be raised by addition of agents capable of inhibiting hydrophobic interactions, including buffers containing arginine and/or ethylene glycol, to the mixture, either prior to adding the mixture to the column chromatography substrate, after adding the mixture to the column chromatography substrate, or both prior to and after adding the mixture to the column chromatography substrate.

Abstract: A process is provided for the preparation of albumin which has extremely low levels of or is essentially free of colorants, metal ions, human proteins, host proteins, fragments of albumin, polymers or aggregates of albumin and viruses, and which is essentially non-glycated, relatively high in free thiol and with an intact C-terminus. The process comprises passing albumin (preferably expressed and secreted by transformed yeast) through positive mode cation exchange and then positive mode anion exchange chromatography. Other steps may also be employed, ultrafiltration, gel permeation chromatography, affinity chromatography binding the albumin by using blue dyes) and affinity chromatography binding contaminants by using an aminophenylboronic acid resin. Elution of albumin, with a compound having affinity for albumin, from a material having no specific affinity for albumin is also disclosed, as is removal of ammonium ions with a counter-ion.

Abstract: A glycoprotein extracted from the fruiting body of Grifola frondosa is demonstrated to have antidiabetic, antihypertensive, antiobesity and antihyperlipidemic effects, and has great potential as an active component for pharmaceuticals, dietary supplements or health food preparations to treat and/or prevent the above diseases. This invention is to provide the glycoprotein and its preparation method.

Abstract: The present invention relates to a method of purifying a protein of interest from its fusion analog, comprising obtaining a protein solution comprising a protein of interest and its fusion analog; adjusting the pH and/or ionic strength of the protein solution with an appropriate buffer for use with a Hydrophobic Charge Induction Chromatograph (HCIC) resin, contacting the protein solution and HCIC resin column to allow binding of the protein of interest and its fusion analog, washing the resin and eluting the protein of interest from the resin by a pH gradient; wherein the protein of interest is substantially free of its fusion analog.

Abstract: The present invention relates to use of Narp inhibitor in order to promote or enhance recovery from ischemic events, particularly focal ischemia of the central nervous system, as well as for preventing or diminishing chronic degenerative changes.

Abstract: This invention relates to the application of hydrophobic interaction chromatography combination chromatography to the purification of antibody molecule proteins.The questions raised in reexamination request, 09/006,966 filed Mar. 12, 2004 have been considered and the results thereof are reflected in this reissue patent which constitutes the reexamination certificate required by 35 U.S.C. 307 as provided in 37 CFR 1.570(e), for ex parte reexaminations, or the reexamination certificate required by 35 U.S.C. 316 as provided in 37 CFR 1.997(e) for inter partes reexaminations.