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biological source
human
recombinant
expressed in E. coli
form
lyophilized
mol wt
~5 kDa
packaging
pkg of 20 μg
storage condition
avoid repeated freeze/thaw cycles
impurities
endotoxin, tested
NCBI accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... DEFB103A(414325)
General description
β-defensin-3 (BD-3) is an anti-microbial peptide produced by airway epithelial cells, lung-derived epithelial cells and keratinocytes. It has a molecular weight of 5kDa. The gene encoding this protein is localized on human chromosome 8p23.1. Recombinant human β-defensin-3 (BD-3) is an antimicrobial peptide, which belongs to the distinct family of β-defenisns. Recombinant human BD-3 is a 5.1 kDa protein containing 45 amino acid residues.
Chemical structure: peptide
Biochem/physiol Actions
β-defensin-3 (BD-3) associates with bacterial products which reduce the effect of inflammatory cytokine responses. The protein has been shown to stimulate the production of interferon-α and activate monocytes through toll-like receptors 1 and 2. It antagonizes the activation of C-X-C motif chemokine receptor 4 (CXCR4).
Physical form
Sterile filtered and lyophilized with no additives.
Reconstitution
Centrifuge the vial prior to opening. Avoid freeze-thaw cycles.
Reconstitute in 10 mM Acetic acid to a concentration of 0.1-1.0 mg/mL. This solution can then be diluted into other aqueous buffers.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Certificates of Analysis (COA)
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Jeffrey P Meisch et al.
Inflammatory bowel diseases, 19(5), 942-953 (2013-03-21)
Antimicrobial peptides (AMPs) maintain a sterile environment in intestinal crypts, limiting microbial colonization and invasion. Decreased AMP expression is proposed to increase the risk for inflammatory bowel disease. Expression and function of inducible AMPs, human β-defensin 2 and 3 (hBD-2
Edward J Hollox et al.
Nature genetics, 40(1), 23-25 (2007-12-07)
Psoriasis is a common inflammatory skin disease with a strong genetic component. We analyzed the genomic copy number polymorphism of the beta-defensin region on human chromosome 8 in 179 Dutch individuals with psoriasis and 272 controls and in 319 German
J Harder et al.
The Journal of biological chemistry, 276(8), 5707-5713 (2000-11-22)
The growing public health problem of infections caused by multiresistant Gram-positive bacteria, in particular Staphylococcus aureus, prompted us to screen human epithelia for endogenous S. aureus-killing factors. A novel 5-kDa, nonhemolytic antimicrobial peptide (human beta-defensin-3, hBD-3) was isolated from human
Stefanie Scharf et al.
Respiratory research, 11, 93-93 (2010-07-10)
Legionella pneumophila is an important causative agent of severe pneumonia in humans. Human alveolar epithelium and macrophages are effective barriers for inhaled microorganisms and actively participate in the initiation of innate host defense. The beta defensin-3 (hBD-3), an antimicrobial peptide
Zhimin Feng et al.
The FEBS journal, 280(14), 3365-3375 (2013-05-11)
Previously, we reported that human β-defensin (hBD)-3 can both antagonize CXCR4 function on T cells and promote receptor internalization in the absence of activation. In the present study, we explored the important structural elements of hBD-3 that are involved in
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