Three letter code
Peptide Purity (HPLC)
Dermaseptin sVIII has only one site of amino acid substitution when compared with dermaseptin sI. Unlike dermaseptin s1, mature dermaseptin sVI–sVIII peptides lacked the C-terminal tripeptide (-GE/AQ) of the precursor openreading frame deduced from their respective cDNAs. MS/ MS fragmentation of each peptide using a QTOF-Ultima instrument (Micromass, UK), established that each was C terminally amidated with either an isoleucine amide (sVI) or a glutamine amide (sVII–sVIII). The defensive skin secretions of frogs are known to contain a plethora of biologically active peptides, some of which share common primary structural features with endogenous vertebrate regulatory peptides and others that appear to have no obvious structural counterparts in higher vertebrates. The dermaseptins constitute a group of peptides that fall into the latter category displaying broad spectrum antimicrobial activity against both bacteria and fungi The role of this peptide family, typically consisting of 27–34 amino acid residues, is thought to be in defending the naked moist skin of the frogs against environmental or pathogenic microbial invasion. One must bear in mind that the integument of the amphibian plays many important physiological roles including respiration and osmoregulation—fundamental processes that could impinge upon the well-being of the animal if impaired by microbial colonisation. In fact, dermaseptins were the first vertebrate peptides to exhibit lethal effects against the filamentous fungi responsible for severe opportunistic infections accompanying immunodeficiency syndrome and the use of immunosuppressive agents.
Ideally Dermaseptin-S8 peptide should be stored in a freezer at or below -9C. Dermaseptin-S8 peptide should be refrigerated after reconstitution. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides
- Chen T, Tang L, Shaw C. Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-sVIII) by cloning from a skin secretion-derived cDNA library. Regul Pept. 2003;116(1-3):139-46
About TFA salt
Trifluoroacetic acid (TFA) is a strong acid, which is commonly used to cleave synthesized peptides from solid-phase resins and is also used to improve HPLC performance in the peptide purification step. By default, custom peptides are delivered as lyophilized TFA salts, and can contain as much as 10-45% TFA.
TFA in custom peptides can cause inexplicable discrepancies in subsequent assay data. For instance, TFA in nM concentrations has been shown to interfere with cellular assays, inhibiting cellular proliferation in some instances, and increasing cell viability in others . It has also been found to be an unintended allosteric modulator of the glycine receptor, GlyR.
TFA Removal Service is recommended for:
- Peptides that will be used in cellular assays
- Peptides that will be used as APIs or in manufactured products
- For hydrophilic peptides containing numerous basic residues
- Analysed Sequence:H-ALWKTMLKKLGTVALHAGKAALGAAADTISQ-Amidation
- Chemical Formula:C141H240N40O38S
- Sequence length:31
- Extinction coefficient:5690 M-1cm-1
- Mw average:3135.71
- Theoretical pI:10.55
- Data Source:Peptide Property Calculator
GRAVY = grand average of hydropathy
X: Hydrophobic uncharged residues, like F I L M V W A and P
X: Basic residues, like R K H
X: Acidic residues, like D E
X: Polar uncharged residues, like G S T C N Q and Y
Related Products / Services
• Peptide Services: NovoPro's peptide synthesis services include standard chemical peptide synthesis, peptide modification, peptide libraries, and recombinant peptide expression.
• Standard Peptide Synthesis: NovoPro offers quality peptides at the most competitive prices in the industry, starting at $3.20 per amino acid. NovoPro provides PepBox – Automatic Quote Tool for online price calculation.
• Peptide Modifications: NovoPro offers a wide range of peptide modification services including isotope labeling (2H, 15N, and 13C), multiple disulfide bonds, multiple phosphorylations, KLH, BSA, ovalbumin, amidation, acetylation, biotin, FITC, etc.
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