Recombinant chemokines chemokine fold

Figure 1 Recombinant chemokine production reproduces the natively folded bioactive protein secreted from eukaryotic cells. (A) Folding, transport, and secretion of chemokines in eukaryotic cells. (B) Schematic diagram of expression, purification, and refolding of recombinant chemokines from coli. (C) The 3D structure of human CXCL12 illustrates the conserved chemokine fold with structurally important disulfide bonds and functionally important native N-terminus.

In conclusion, the supply of pure, natively folded chemokine proteins is vital for a variety of basic, translation and cHnical research programs. Our structure-function studies and drug development efforts have motivated the development of the robust protocol for recombinant chemokine expression, refolding, purification, and vahdation presented here. Finally, many additional factors must be considered when manufacturing a product under cGMP guidehnes that may not be obvious to personnel in research settings. 

A supply of bioactive chemokine protein is essential to the study of chemokine function and to be fuUy active the protein must be properly folded. Figure 1 illustrates the differences in natural eukaryotic and recombinant bacterial production of chemokines, each of which is optimized to yield a natively folded, bioactive protein. 

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