Recombinant Human BD-3 protein

Background

Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 k Da proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Four human β-defensins have been identified and they are expressed on some leukocytes and at epithelial surfaces. Because β-defensins is cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane.

Expression system

Escherichia coli.

Purity

> 98 % by SDS-PAGE and HPLC analyses.

Molecular weight

Approximately 5.2 kDa, a single non-glycosylated polypeptide chain containing 45 amino acids.

Endotoxin

Less than 1 EU/μg of rHuBD-3 as determined by LAL method.

Form

Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 130 mM NaCl.

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