Alternative names for Cecropin-B antibody
Enzyme Immunoassay (E), Immunoprecipitation (IP), Western blot / Immunoblot (WB)
Background of Cecropin-B antibody
Cecropins are produced by insects, particularly under conditions of infection. Cecropins are bioactive peptides that exhibit activities by interacting with membranes and forming transmembrane channels that allow the free flow of electrolytes, metabolites and water across the phospholipid bilayers. Cecropins A, B and D are close homologues consisting of 35-39 residues. They are found in the pupae of the cecropin moth, but related homologues named lepodopteran, bactericidin, moricin and sarcotoxin are produced by other insects.
Bechinger B Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J Membr Biol 156:197-211 (1997). PubMed: 9096062.
Kato Y et al. Expression and characterization of cDNAs for cecropin B, an antibacterial protein of the silkworm, Bombyx mori. Insect Biochem Mol Biol 23:285-90 (1993). PubMed: 8485525
Brey PT et al. Role of the integument in insect immunity: epicuticular abrasion and induction of cecropin synthesis in cuticular epithelial cells. Proc Natl Acad Sci U S A 90:6275-9 (1993). PubMed: 8327509.
Taniai K et al. Isolation and nucleotide sequence of cecropin B cDNA clones from the silkworm, Bombyx mori. Biochim Biophys Acta 1132:203-6 (1992). PubMed: 1390892.
Gudmundsson GH et al. The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia. J Biol Chem 266:11510-7 (1991). PubMed: 1711035
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