BD-1 (47aa)

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. Beta-defensins are expressed on some leukocytes and at epithelial surfaces. 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 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. Recombinant Human BD-1 is a 5.0 kDa protein containing 47 amino acid residues.

DEFB1; BD1; HBD1; DEFB-1; DEFB101

1672

P60022

NP_5209.1

NM_005218

8p23.1

Human

Human

GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK

< 0.1 ng/µg of protein (< 1EU/µg)

> 98% by SDS-PAGE & HPLC analyses

Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000 ng/ml.

47

Lyophilized

5.0 kDa

E. coli