Evasins are a family of >50 chemokine binding anti-inflammatory proteins identified in the saliva of some species of ticks. EVA-ACA1001, EVA-P974 and EVA-AAM1001 have been identified as promiscuous CC chemokine binders with affinity for almost all CC chemokines. We believe their promiscuity makes them a promising potential treatment for inflammatory diseases. As evasins are small proteins (~13kDa) their half-life in vivo is of critical concern for drug development. Despite this, very little is known about their pharmacokinetics. To improve the half-life of evasins we have produced fusion proteins using the XTEN fusion partner, originally developed by Schellenberger et al. XTEN is an unstructured polypeptide chain that can be produced at various lengths to scale the hydrodynamic volume of the protein of interest. Here we detail the expression, purification, functional validation, and pharmacokinetic analysis of three different length XTEN fusion to our evasins of interest.