PR11



BML-PW9325-0100	100 µg	108.00 USD

Studies have demonstrated that PR39, a proline/arginine rich 39 amino acid antibacterial peptide originally derived from porcine bone marrow, exhibits a broad spectrum of biological activities, including the ability to induce angiogenesis and to limit inflammatory damage in a variety of animal models. The angiogenic effect is in part explained by the ability of PR39 to inhibit proteasome-dependent degradation of the transcription factor HIF-1a, while anti-inflammatory activity is associated with inhibition of IκBα degradation that in turn prevents activation of NFκB-dependent gene expression.

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Product Specification

Alternative Name:	N-terminal undecapeptide of PR39

MW:	1463.7

Purity:	≥95% (HPLC)

Sequence:	Arg-Arg-Arg-Pro-Arg-Pro-Pro-Tyr-Leu-Pro-Arg

Solubility:	Soluble in water

Long Term Storage:	-20°C

Background / Technical Information:	Please click here for the comprehensive product datasheet.

Product Literature References

PR-39 and PR-11 peptides inhibit ischemia-reperfusion injury by blocking proteasome-mediated IkBα degradation: J. Bao et al.; Am. J. Physiol. Heart Circ. Physiol. 281, 2612 (2001),

Inhibition of ubiquitin-proteasome pathway-mediated I kappa B alpha degradation by a naturally occurring antibacterial peptide: Y. Gao et al.; J. Clin. Invest. 106, 439 (2000), Abstract;

PR39, a peptide regulator of angiogenesis: J. Li et al.; Nat. Med. 6, 49 (2000), Abstract;

Macrophage-dependent regulation of syndecan gene expression: J. Li et al.; Circ. Res. 81, Nov (1997), Abstract;

PR-39, a proline-rich peptide antibiotic from pig, and FALL-39, a tentative human counterpart: B. Agerberth et al.; Vet. Immunol. Immunopathol. 54, 127 (1996), Abstract;

Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39: G. H. Gudmundsson et al.; PNAS 92, 7085 (1995), Abstract;

Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds: R. L. Gallo et al.; PNAS 91, 11035 (1994), Abstract;

Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine: H. G. Boman et al.; Infect. Immun. 61, 2978 (1993), Abstract;

Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides: B. Agerberth et al.; Eur. J. Biochem. 202, 849 (1991), Abstract;