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BML-PW9325-0100 100 µg 170.00 USD
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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. The activities of PR39 reside in the N-terminal portion of the molecule encompassed by PR11. The most recent findings have demonstrated that PR39 is a non-competitive and reversible inhibitor of the proteasome function, which is achieved by a unique allosteric mechanism allowing for specific inhibition of degradation of selected proteins without affecting total proteasome-dependent proteolysis. A proline-arginine-rich 11 amino acid peptide derived from the naturally occurring peptide antibiotic PR39. PR39 has been shown to act as an inhibitor of both 20S and 26S proteasomes with proposed selectivity for the inhibition of the degradation of IκBα, HIF-1a and certain other proteins. PR39 has been reported to inhibit the proteasomal degradation of IκBα without effecting overall proteasome activity, or degradation of p21Cip1/Waf1 and c-fos, cell-cycle genes regulated by proteasome-dependent degradation. In vitro studies have demonstrated PR39 to be an efficient inhibitor of all three activities of the 20S proteasome. Unlike MG132 and lactacystin, long-term exposure to PR39 shows little toxicity or induction of HSP-70. In mouse models of myocardial infarction it has been shown that infusion with PR11 results in a significant reduction of myocardial infarct size. PR39, PR11 and related peptides may therefore provide novel means to regulate cellular function and the control of NF-κB-dependent gene expression for therapeutic purposes.

Product Details

Alternative Name:N-terminal undecapeptide of PR39
Purity:≥95% (HPLC)
Solubility:Soluble in water
Shipping:Blue Ice
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only

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;

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