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Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils.
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The epididymis-specific expression pattern of the beta-defensin isoform mBD-6 has been characterized.
Unique properties of human beta-defensin 6 (hBD6) and glycosaminoglycan complex: sandwich-like dimerization and competition with the chemokine receptor 2 (CCR2) binding site.
DEFB106 (also known as DEFB6) displays antimicrobial activity against E. coli, C. albicans and S. aureus.
The epididymis-specific expression pattern of the beta-defensin isoform BD-6 has been characterized.
A pilot study with cRNA probes for in situ hybridization and a synthetic propeptide for the functional characterization demonstrated the tissue-/cell-specific expression and the strong antimicrobial activity of DEFB106
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Defensins are short, processed peptide molecules that are classified by structure into three groups: alpha-defensins, beta-defensins and theta-defensins. All beta-defensin genes are densely clustered in four to five syntenic chromosomal regions. Chromosome 8p23 contains at least two copies of the duplicated beta-defensin cluster. This duplication results in two identical copies of defensin, beta 106, DEFB106A and DEFB106B, in head-to-head orientation. This gene, DEFB106B, represents the more telomeric copy.
, Beta-defensin 6
, bovine neutrophil beta-defensin 3
, defensin beta 3
, beta-defensin 106
, defensin, beta 6
, defensin, beta 106