Recombinant Human BD-2

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, four human beta-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. In addition to their direct antimicrobial activities, they are chemoattractant 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 the case of BD-1, a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.

Human, rabbit and guinea-pig beta-defensins, as well as human beta-defensin-2 (hBD2), induce the activation and degranulation of mast cells, resulting in the release of histamine and prostaglandin D2.