Recombinant Human BD-1 (47 a.a.) 0 ReviewsSubmit a Review Product Details Catalogue Number: 300-51A Description: Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. 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 some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-1 is a 5.0 kDa protein containing 47 amino acid residues. Source: E.coli Synonyms: Beta-Defensin 1, DEFB1, HBD1 AA Sequence: GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses. Biological Activity: Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100.0-1000.0 ng/ml. Calculated Molecular Weight: 5 kDa Accession Number: P60022 Gene ID: 1672 Endotoxin: Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug) crossreactivity: Human References PubMed SDS CoA Search Product Line Country Of Origin: USA Not for human use. Research Interest Chemotaxis Immune System Stem Cells & Differentiation product.subtitle.recentcitations First Author Wilson, C L Title Differential Processing of {alpha}- and {beta}-Defensin Precursors by Matrix Metalloproteinase-7 (MMP-7). Citation The Journal of Biological Chemistry; 284(13) pg8301-11 PubMed Id 19181662 First Author Schibli, D J Title The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. Citation The Journal of Biological Chemistry; 277(10) pg8279-89 PubMed Id 11741980