Human beta-Defensin 3 Antibody
Human beta-Defensin 3 Antibody Summary
Accession # P81534
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: beta-Defensin 3
beta -Defensin 3, also known as BD3 and DEFB-3, is a membrane-active cationic peptide that functions in inflammation and innate immune responses. There are at least 30 beta ‑Defensins which are distinguished from alpha ‑Defensins by the connectivity pattern of their three intramolecular disulfide bonds (1). The 45 amino acid (aa) mature human BD3 shares 38% and 33% aa sequence identity with mouse and rat BD3, respectively (2, 3). It shares 18%‑36% aa sequence identity with other human beta ‑Defensins. BD3 is widely expressed among epithelial tissues, notably by keratinocytes and airway epithelial cells. It is up‑regulated in response to proinflammatory cytokines, microbial and viral infections, and at the edges of skin wounds (2, 4‑6). BD3 induction in osteoarthritis chondrocytes promotes MMP1 and 13 production and inhibits TIMP1 and 2 expression (7). In vivo control of BD3 activity is accomplished in part through cleavage by cathepsins B, L, and S (8). BD3 displays strain specific microbicidal activity toward a broad spectrum of bacteria and yeast (2, 9). BD3 also induces monocyte migration, mast cell activation, and a mast cell‑dependent increase in vascular permeability (4, 10). Disruption of the intramolecular disulfide bond pattern in BD3 abrogates its monocyte chemoattractant properties but not its antimicrobial properties (11, 12). BD3 inhibits viral infectivity by interacting directly with HIV-1 plus its coreceptor CXCR4 (5, 13), and with HSV glycoprotein B plus its receptor heparan sulfate (14), and by forming a protective coating on the surface of influenza virus target cells (15).
- Dhople, V. et al. (2006) Biochim. Biophys. Acta 1758:1499.
- Harder, J. et al. (2001) J. Biol. Chem. 276:5707.
- Schibli, D.J. et al. (2002) J. Biol. Chem. 277:8279.
- Garcia, J.-R.C. et al. (2001) Cell Tissue Res. 306:257.
- Quinones-Mateu, M.E. et al. (2003) AIDS 17:F39.
- Sorensen, O.E. et al. (2006) J. Clin. Invest. 116:1878.
- Varoga, D. et al. (2005) Arthritis Rheum. 52:1736.
- Taggart, C.C. et al. (2003) J. Immunol. 171:931.
- Joly, S. et al. (2004) J. Clin. Microbiol. 42:1024.
- Chen, X. et al. (2007) Eur. J. Immunol. 37:434.
- Kluver, E. et al. (2005) Biochemistry 44:9804.
- Wu, Z. et al. (2003) Proc. Natl. Acad. Sci. 100:8880.
- Feng, Z. et al. (2006) J. Immunol. 177:782.
- Hazrati, E. et al. (2006) J. Immunol. 177:8658.
- Leikina, E. et al. (2005) Nat. Immunol. 6:995.
Citation for Human beta-Defensin 3 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Inactivation of HIV-1 in Polarized Infant Tonsil Epithelial Cells by Human Beta-Defensins 2 and 3 Tagged with the Protein Transduction Domain of HIV-1 Tat
Authors: R Herrera, K Rosbe, SM Tugizov
Sample Types: Cell Ly
Applications: Western Blot
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