[5-FAM]-CRAMP (6-39)
[5-FAM]-GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ-acid
Description
Application Data
Description
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Potent anti-microbial peptide against Gram-positive and Gram-negative bacteria with N-terminal fluorescent tag.
Application Data
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Catalogue number crb1100256 Molecular Weight 4236.91 Sequence (one letter code) [5-FAM]-GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ-acid
Sequence (three letter code) [5-FAM]-Gly-Leu-Leu-Arg-Lys-Gly-Gly-Glu-Lys-Ile-Gly-Glu-Lys-Leu-Lys-Lys-Ile-Gly-Gln-Lys-Ile-Lys-Asn-Phe-Phe-Gln-Lys-Leu-Val-Pro-Gln-Pro-Glu-Gln-OH
Purity >95% References Horibe et al (2013) Roles of cathelicidin-related antimicrobial peptide in murine osteoclastogenesis. Immunology 40(3) 344 PMID: 23826736
Santos et al (2013). Endogenous cathelicidin production limits inflammation and protective immunity to Mycobacterium aviumin mice. Immun. Inflamm. Dis. 2(1) 1 PMID: 25400920
Manufactured in: United Kingdom Amino acids 6-39 of the cathelicidin-related anti-microbial peptide (CRAMP), the mouse homologue of the human LL-37 anti-microbial peptide.
CRAMP possesses potent anti-bacterial activity against Gram-positive and Gram-negative bacterial strains with no haemolytic activity. As well as displaying direct anti-microbial activity, CRAMP also binds to lipopolysaccharide (LPS) to neutralise its activity.
CRAMP is a cationic peptide, encoded for by the Camp gene and is highly expressed in bone marrow. Its expression is up-regulated by infectious and inflammatory signals and it is secreted by cells such as neutrophils epithelial cells and macrophages.
This peptide contains N-terminal 5-Carboxyfluorescein (5-FAM), a widely used, green fluorescent tag
[5-FAM]-CRAMP (6-39)
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