Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are distinguished from the beta-defensins by the pairing of their three disulfide bonds. To date, six human beta-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-2 is a 4.3 kDa protein containing 41 amino acid residues.