Alpha-Defensin-2 (Human)

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Alpha-Defensin-2 (Human)
α-Defensin-2 | HNP-2 (Human Neutrophil Peptide-2)

4428-s 0.1 mg | 140.00 EUR

Synthetic Product (disulfide bonds between Cys1-Cys29, Cys3-Cys18 and Cys8-Cys28)

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

(M.W. 3371.0) C147H217N43O37S6

The purity of alpha-defensin-2 is guaranteed to be higher than 99% by HPLC

Antimicrobial Peptide are a family of 6 peptides: 4 human neutrophil peptides [HNP-1, HNP-2, HNP-3, HNP-4] and 2 human defensins [HD-5 and HD-6]. Among them, the primary structures of HNP-1, HNP-2 (Alpha-Defensin-2) and HNP-3 differ only at the amino-terminal residue, in which the first residue is Ala for HNP-1 and Asp for HNP-3, whereas HNP-2 lacks this position, resulting in the 29-residue peptide. Recent studies in mass spectroscopic analysis clarified that Alpha-Defensin-2 (Human) is the second major component in squamous cell carcinoma of human tongue and gingival crevicular fluid from periodontitis patients and healthy controls, where HNP-1 is the most abundant and HNP-3 is the least. Taking this fact into account, it is speculated that HNP-2 is produced post-translationally from HNP-3. Concerning the activity, HNP-2 (Alpha-Defensin-2) is revealed to be as active as HNP-1 in neutralizing anthrax lethal toxin and blocking papillomavirus infection, although some differences were pointed out in the candidacidal activity among HNPs. Anyhow HNP-2 has now been added to our catalog, in addition to HNP-1 and HNP-3. Thus more precise experiments will be possible to eludicidate the biological roles of the individual peptides of co-existing HNP-1, HNP-2 and HNP-3 in the body.

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)
  2. M.E. Selstedt, S.S.L. Harwig, T. Ganz, J.W. Schilling and R.I. Lehrer, J. Clin. Invest., 76, 1427 (1985) (Original; Structure)
  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.; HNP in Gingival Crevicular Fluid)
  4. C. Kim, N. Gajendran, H.W. Mitrüker, M. Weiwad, Y.H. Song, R. Hurwitz, M. Wilmanns, G. Fischer and S.H.E. Kaufmann, Proc. Natl. Acad. Sci. USA, 102, 4830 (2005) (Pharmacol.; Neutralisazion of Anthrax Lethal Toxin)
  5. C.B. Buck, P.M. Day, C.D. Thompson, J. Lubkowski, W. Lu, D.R. Lowry and J.T. Schiller, Proc. Natl. Acad. Sci. USA, 103, 1516 (2006) (Pharmacol.; Inhibition of Papillomavirus Infection)
  6. R.I. Lehrer, T. Ganz, D. Szklarek and M.E. Selstedt, J. Clin. Invest., 81, 1829 (1988) (Pharmacol.; Activity difference in HNP)

Links to publications that used our peptide alpha-Defensin-2 | code 4428-s:

  1. The Virulence Regulator Sae of Staphylococcus aureus: Promoter Activities and Response to Phagocytosis-Related Signals

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