Alpha-Defensin-3 (Human)
α-Defensin-3 | HNP-3 (Human Neutrophil Peptide-3)

4416-s 0.1 mg | 140.00 EUR

Synthetic Product (disulfide bonds between Cys²-Cys³⁰, Cys⁴-Cys¹⁹ and Cys⁹-Cys²⁹)

Asp – Cys – Tyr – Cys – Arg – Ile – Pro – Ala – Cys – Ile – Ala – Gly – Glu – Arg – Arg – Tyr – Gly – Thr – Cys – Ile – Tyr – Gln – Gly – Arg – Leu – Trp – Ala – Phe – Cys – Cys

The purity of alpha-Defensin-3 is guaranteed to be higher than 99% by HPLC

Antimicrobial Peptide

Defensin is one of the potential protecting factors against microbial infection. In human, α-Defensins (Alpha-Defensin) and β-Defensins (Beta-Defensin) are known, which are characterized by their distinct arrangement of three disulfide bridges.
To date, six human α-Defensins are classified into two sub-groups: one group is composed of human neutrophil peptides (HNP), HNP-1 to HNP-4, and the other group is human defensin (HD), HD-5 and HD-6. In addition to human alpha-defensin-1 (HNP-1), we now introduce two new members of the Defensin family, alpha-Defensin-3 (HNP-3) and human alpha-defensin-5 (HNP-5).
HNP-1 to HNP-3 are the major components in azophilic granules of human neutrophils. The primary structures of HNP-1 to HNP-3 differ by only one amino acid residue at position 1; HNP-2 corresponds to position 2 through 30 of HNP-1 while HNP-3 is Asp¹-HNP-1. Recent interesting publications using HNP include i) HNP-1 to HNP-3 are secreted upon stimulation of CD8 cells from non-progressors of HIV-1 infection, thus, these three peptides may show anti-HIV-1 activity, and ii) HNP-1 to HNP-3 are overexpressed in squamous cell carcinomas of the human tongue, representing a possible role in innate host defense against tumor invasion. It has been reported that expression of HNP-1 to HNP-3 is not upregulated by lipopolysaccharide, while they locate in intestinal epithelian cells in cases of inflammatory bowel disease.

References:

1. T. Ganz, M.E. Selstedt, D. Szklarek, S.S.L. Harwig, K. Daher, D.F. Bainton and R.I. Lehrer, J. Clin. Invest., 76, 1427 (1985) (Original; Isolation of HNP 1-3)
2. M.E. Selstedt, S.S.L. Harwig, T. Ganz, J.W. Schilling and R.I. Lehrer, J. Clin. Invest., 76, 1436 (1985) (Original; Structure of HNP 1-3)
3. F.T. Lundy, D.F. Orr, J.R. Gallagher, P. Maxwell, C. Shaw, S.S. Napier, C.G. Cowan, P.J. Lamey and J.J. Marley, Oral. Oncol., 40, 139 (2004) (Pharmacol.; Role in Tumor Invasion)