Using this technology, the company’s scientists have produced a large number of active and authentic human cytokine and kinase reagents designed to meet the needs of researchers. Comparative studies indicate that these recombinant human proteins from human cells are superior to those produced in nonhuman cell systems.
Most human cytokines are glycoproteins less than 30 kD in size. Due to their central role in the immune system, cytokines are involved in a variety of immunological, inflammatory, and infectious diseases and are widely used in research, diagnostics, and therapeutics. Currently, these proteins are predominantly produced in nonhuman cell-expression systems (e.g., E. coli, SF9, or CHO) and therefore lack authenticity due to the absence of physiologically relevant glycosylation.
Additionally, a number of important cytokines such as those belonging to the TGF-b superfamily are difficult to produce in sufficient quantity due to inadequate proteolytic processing, protein folding, or other post-translational modifications that occur in the nonhuman cell-expression systems.
HumanZyme’s work with VEGF165 and IL-4 demonstrates that the recombinant cytokines from human cells are differentiated from the nonhuman-cell version and can be used as preferred reagents for research and antibody development.
VEGF165 plays a prominent role in normal and pathological angiogenesis. It has been demonstrated that inhibition of VEGF activity by treatment with a mAb specific for VEGF can suppress tumor growth in vivo. Currently, commercially available VEGF165 protein reagents are produced from nonhuman cells including E. coli and insect cells.