Described herein is a surge tank based system to control surge tanks in a manufacturing train. The system includes data acquisition unit, data normalization unit, deviation identification and handling unit and an real time execution of control action from centralized computer in a manufacturing process unit, wherein said manufacturing unit includes an integrated system which incorporates a plurality of pumps, surge tanks, and weighing balances, and other unit operations alongside the normal unit operations of production of output product.

The present invention is directed to the identification of a biomarker specifically located in the plasma membrane of pancreatic beta cells. Based on a set of specific features the biomarker is a unique candidate for imaging and targeting strategies to study the pancreatic beta cell mass in health and disease (T1D, T2D, pancreatic cancers, obesity, islet transplantation, beta cell regeneration).

The present invention relates to the use, for affinity purification of an antibody or an fragment of an antibody, of a ligand-substituted matrix comprising a support material and at least one ligand covalently bonded to the support material, the ligand being represented by formula (I)
L-(Sp).sub.v-Ar.sup.1—Am—Ar.sup.2   (I)
wherein L, SP, Ar.sup.1, AM, Ar.sup.2 and v are defined herein.

Provided is a method for control and/or monitoring and/or optimization of a chromatographic process, in which the method comprises at least 2 columns which are operated, alternatingly, wherein this operation can be carried out in that the at least 2 columns are operated in interconnected and disconnected states, wherein the columns switch positions after such a sequence of interconnected and disconnected state, and wherein downstream of at least one, or of each column, a detector is located capable of detecting the desired product and/or impurities when passing the detector.

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.

The present invention is directed to an affinity chromatography device that has a normal flow and which separates a targeted protein from aqueous mixtures. The chromatography device includes a housing containing therein a spiral wound membrane assembly that includes at least one inner intermediate material that forms an outer flow channel, at least one polymer membrane that contains therein inorganic particles, and at least one outer intermediate material that forms an inner flow channel sequentially positioned around a central core having a solid outer wall. An aqueous mixture is passed through the outer flow channel, through the polymer membrane where the targeted protein is removed, and then through an inner flow channel. The affinity chromatography device further includes an inlet flow distributor containing an inlet and an outlet flow distributer containing an outlet. Additionally, the chromatography device has a dimensionless resistance parameter that is less than 0.08.

High resolution affinity chromatography combining affinity resolving and affinity capture processes using a single chromatography matrix results in improved resolution between closely related molecular species and significantly enhances overall product yield for large scale commercial production of heterodimeric proteins such as bispecific antibodies. Moreover, tankage and equipment requirements are reduced via the ability to reduce salt concentration, while increasing product purity and concentration, without the need for dilution, ultrafiltration or diafiltration.

The present invention addresses the problem of providing FcRn having improved stability with respect to heat and acids, a method for producing said FcRn, an antibody adsorbent in which said FcRn is used, and an antibody isolation method in which said adsorbent is used. The above problem is solved by substituting an amino acid residue at a specific position in an extracellular region of a human FcRn α chain and/or a β2 microglobulin region of a human FcRn β chain by another specific amino acid.

The invention concerns polymeric media based on modified natural polysaccharides for removing one or both of Anti-A Antibodies and Anti-B Antibodies from human blood or plasma, the media comprising one or both of (i) a polymeric solid support with a blood group A Antigen ligand attached to the solid support at a ligand loading between 1-5 mg/mL of solid support, and wherein the media is stable under physiological pH conditions, and (ii) a polymeric solid support with a blood group B Antigen ligand attached to the solid support at a ligand loading between 1-5 mg/mL of solid support, and wherein the media is stable under physiological pH conditions.

Provided herein are, inter alia, biological manufacturing and downstream purification processes.