Abstract: A magnetic particle separation system includes a magnetic field generating device having an upper surface with a receiving area formed thereon; and a magnetic field generating element disposed beneath the upper surface, the magnetic field generating element being configured to produce a magnetic field above the upper surface. A container assembly is disposed on the upper surface and includes: a flexible container having an outer wall with an interior surface that at least partially bounds an internal compartment, the outer wall having a front side and an opposing back side with the internal compartment disposed therebetween; a fluid inlet extending through the outer wall at the front side; a fluid outlet extending through the outer wall at the front side; and a first partition projecting into the internal compartment from the front side between the fluid inlet and the fluid outlet.

Abstract: Provided are methods and composition useful in isolating or otherwise preparing a population of target cells. In part, it relates to recombinant antibodies comprising an exogenous proteolytic cleavage site and nucleic acid molecules encoding the antibodies.

Abstract: Provided are methods and composition useful in isolating or otherwise preparing a population of target cells. In part, it relates to recombinant antibodies comprising an exogenous proteolytic cleavage site and nucleic acid molecules encoding the antibodies.

Abstract: Methods of reversal of the binding between a biotin compound and a biotin-binding compound are disclosed. A method of reversibly releasing a biotinylated moiety from a streptavidin (or avidin) coated support is shown as an example. The strong interaction between streptavidin or avidin-biotin is made much weaker by using a combination of modified streptavidin or avidin and modified biotin like desthiobiotin or a derivative thereof like DSB-X Biotin. A protein, such as an antibody may be biotinylated with the modified biotin. When this protein is isolated by binding the modified biotin to the modified streptavidin or avidin bound to an solid surface, it may be released under very gently and very rapid conditions by addition of free biotin. In contrast to proteins obtained by the prior art release methods the protein obtained using the previously available release methods, the proteins obtained using the methods disclosed herein will maintain their native conformation.

Abstract: Methods of reversal of the binding between a biotin compound and a biotin-binding compound are disclosed. A method of reversibly releasing a biotinylated moiety from a streptavidin (or avidin) coated support is shown as an example. The strong interaction between streptavidin or avidin-biotin is made much weaker by using a combination of modified streptavidin or avidin and modified biotin like desthiobiotin or a derivative thereof like DSB-X Biotin. A protein, such as an antibody may be biotinylated with the modified biotin. When this protein is isolated by binding the modified biotin to the modified streptavidin or avidin bound to an solid surface, it may be released under very gently and very rapid conditions by addition of free biotin. In contrast to proteins obtained by the prior art release methods the protein obtained using the previously available release methods, the proteins obtained using the methods disclosed herein will maintain their native conformation.

Abstract: Provided are methods and composition useful in isolating or otherwise preparing a population of target cells. In part, it relates to recombinant antibodies comprising an exogenous proteolytic cleavage site and nucleic acid molecules encoding the antibodies.

Abstract: Provided herein is a bioprocessing device, bioprocessing card, and fluidics cartridge for performing automated bioprocessing of a sample. The bioprocessing card may include a plurality of pipette tips; and at least one pump in fluid communication with the plurality of pipette tips. In some embodiments, the pumps and the pipette tips are in fluid communication through a processing channel which may be a microscale channel. Also provided herein is an automated bioprocessing device comprising: at least one bioprocessing card; at least one fluidic cartridge; and an automated control system configured to control automated bioprocessing of a sample. Further provided herein are methods of use of the device, card, and cartridge.

Abstract: Provided herein is a bioprocessing device, bioprocessing card, and fluidics cartridge for performing automated bioprocessing of a sample. The bioprocessing card may include a plurality of pipette tips; and at least one pump in fluid communication with the plurality of pipette tips. In some embodiments, the pumps and the pipette tips are in fluid communication through a processing channel which may be a microscale channel. Also provided herein is an automated bioprocessing device comprising: at least one bioprocessing card; at least one fluidic cartridge; and an automated control system configured to control automated bioprocessing of a sample. Further provided herein are methods of use of the device, card, and cartridge.

Abstract: Methods of reversal of the binding between a biotin compound and a biotin-binding compound are disclosed. A method of reversibly releasing a biotinylated moiety from a streptavidin (or avidin) coated support is shown as an example. The strong interaction between streptavidin or avidin-biotin is made much weaker by using a combination of modified streptavidin or avidin and modified biotin like desthiobiotin or a derivative thereof like DSB-X Biotin. A protein, such as an antibody may be biotinylated with the modified biotin. When this protein is isolated by binding the modified biotin to the modified streptavidin or avidin bound to an solid surface, it may be released under very gently and very rapid conditions by addition of free biotin. In contrast to proteins obtained by the prior art release methods the protein obtained using the previously available release methods, the proteins obtained using the methods disclosed herein will maintain their native conformation.