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Affinity Depletion Cartridges for Removal of Human Serum Albumin and Immunoglobulins from Human Serum

amples via high throughput Multi Dimensional Liquid Chromatography system such as VISION Workstation as well as processing single samples in a manual mode using unique cartridge format.

Use in conjunction with 2D gels, ICAT reagent technology, LC/MS or MALDI_TOF MS analysis

Experimental Conditions:

In this work, a sample of human serum was passed over both a Protein G and Anti-HSA cartridge. The flow through (serum proteins) and eluted fractions (albumin and IgG) were analyzed by 1 dimensional and 2 dimensional SDS PAGE gel as well as a commercially available ELISA assay, in order to quanitate the removal of HSA and IgG from the sample, and examine the level of non specific binding. Bands from the 1D Gel were further analyzed using peptide mass fingerprinting analysis on the VOYAGER Workstation in order to identify visualized bands that did not correspond to the intact molecular weight of HSA. Comparisons of binding capacities of albumin from different species was also compared to determine cross reactivity.

70 uL samples of human serum diluted 1:10 (7uL undiluted serum) with phosphate buffered saline (PBS) was first passed through a 4mmDx15mmL (0.2mL) Protein G cartridge and then the flow-through fraction was diluted to 400uL. Then 100 uL of the diluted protein G flowthrough fraction was applied to a 4mmDx15mmL (0.2mL) Anti-HSA cartridge at a flow rate of 0.5mL/min. Elution of each cartridge was done using 3 mL of 12mM HCL at 1mL/min and the cartridge was then cleaned with a 5 mL step of 1M NaCl. All chromatographic steps were carried out using the Vision Workstation and the peak flow-through and eluted fractions were collected for further analysis.

Protein concentration for each fraction was determined using Bradford assay. Equal amounts of protein (6.5ug) from each fraction were analyzed by SDS-PAGE and the proteins were visualized by colloidial Coomassi
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