Human Serum Albumin, recombinant (yeast)
Have you ever wondered that if albumin causes your failed experiment?  Numerous literature has shown that the sources and batches of albumin significantly affect their performance. Why is that?
When serum albumin is isolated from serum or recombinant hosts, a handful of bioactive molecules are associated with it. These impurities of albumin cause its lot-to-lot performance variation. Recombinant albumin from non-animal species, on the other hand, is also associated with another set of molecules from the expression host.
We believe that these associated components hold great potentials for advancing modern cell culture techniques. Therefore, we study the small molecule profile of albumin, and formulate highly purified albumin accordingly, to reconstitute albumin's optimum performance for cell culture.
These associated components could also affect albumin's capability to stabilize other proteins in culture medium, such as the growth factors. By defining the impurity profile of albumin, one could better control its effect on cells.
Validated for the Most Demanding Cells
We further believe that every cell type has its preference for albumin. Therefore, we developed and tested our formulated albumin individually on cell types where the chemically defined medium is required.
Our technology has successfully derived albumin optimized for iPS, T-Cell, MSC, and Neuron cultures. As shown below, cells are grown in chemically defined medium with the presence and absence of deAlbumin™, and the difference in viable cell density is plotted.
Culturing condition: T-cell: 5d in CDM as in ref. 1, iPS: 5d in Essential 8, MSC: 5d in CDM as in ref. 2, Neuron: 1 DIV in NS21/Neuronbasal as in ref. 3.
Left: precise control of albumin composition; Bottom: cells cultivated with albumin in chemically defined medium.