Anti-BD3 (beta-Defensin 3)

Antimicrobial peptides are a common mechanism of host defense utilized by a variety of species, from insects to humans. Defensins are a large family of broad-spectrum antimicrobial peptides, identified originally in leukocytes of rabbits and humans. Defensins, cationic/polar peptides (30-35 aa, 3-4kD), are distinguished by conserved tri-disulfides and a largely b-Sheet structure. Defensins, expressed at the cell surface, have been hypothesized to function as a biochemical barrier against microbial infection by inhibiting colonization of the epithelium by wide range of pathogenic microorganisms. In leukocytes, these peptides are stored in cytoplasmic granules and are released into phagolysosomes where they contribute to the killing of engulfed microorganisms. The genes encoding human a- and b-defensins are clustered in a contiguous segment of chromosome 8p23. Defensins are classified into two families designated a- and b- based on distinctive, although similar, tri-disulfide linkages in the peptides. b-defensins are slightly larger and differ in the position and arrangement of 3 disulfides. In humans, six a-defensin (cryptidins), HD1-6 (HD1-4 are also known as HNP1-4 for Human Neutrophil Peptides), and two b-defensins, HBD-1 and HBD-2, have been identified to date. Rat (RBD-1 and RBD-2) and mouse (MBD1-4) homologs of the human beta-defensin have also been identified. Applications: Suitable for use in ELISA. Western Blot, though not tested, may potentially be used as an application. Other applications not tested. Recommended Dilutions: ELISA: 0.5-1ug/ml, Control peptide (Cat.# B0902B) can be used to coat ELISA plates at 1ug/ml., Western Blot: 1-10ug/ml using ECL technique., Optimal dilution determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.