Recombinant Human beta-Defensin 1 Protein

Purity > 98 % by SDS-PAGE and HPLC analyses. Endotoxin level is less than 1EU/µg. Function 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 kDa 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. The β-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-defensin 1 may play a role in the pathogenesis of severe sepsis. Variation in human Beta Defensin-1 contributes to asthma diagnosis, with apparent gender-specific effects. Variation in human β-defensins 1 contributes to asthma diagnosis, with apparent gender-specific effects. Human BD1 is down-regulated in human prostatic and renal carcinomas.

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