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  • OH-CATH

OH-CATH

Cat.#: 314907

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Optional Service: TFA RemovalWhat's this?

Special Price 391.0 USD

Availability: 4 weeks
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Product Information

  • Product Name
    OH-CATH
  • Documents
  • Quantity/Unit
    1 Vial
  • Sequence
    KRFKKFFKKLKNSVKKRAKKFFKKPRVIGVSIPF
  • Three letter code
    Lys-Arg-Phe-Lys-Lys-Phe-Phe-Lys-Lys-Leu-Lys-Asn-Ser-Val-Lys-Lys-Arg-Ala-Lys-Lys-Phe-Phe-Lys-Lys-Pro-Arg-Val-Ile-Gly-Val-Ser-Ile-Pro-Phe
  • Length (aa)
    34
  • Peptide Purity (HPLC)
    97.2
  • Source
    Synthetic
  • Additional Information
    Rich in lysines (35%). Active against E. cloacae (MIC 1 ug/ml), E. aerogenes (MIC 4 ug/ml), E. coli (MIC 6-20 ug/ml), S. aureus (MIC 4 ug/ml), and P. aeruginosa PAO1 (MIC 2 ug/ml). Predicted to be helical based on the known structure of human LL-37. OH-CATH30 is obtained by removing the N-terminal 4 residues. OH-CM6 is obtained by further shortening OH-CATH30 by deleting the C-terminal 10 residues followed by mutations. These derivatives are active against indicator and resistant bacterial strains (MIC in the range of 1.5-25 ug/ml). Activity is reduced in the presence of serum. However, the D-form is stable for at least 12 h. These peptides appear to work on membranes as indicated by rapid killing in 60 min (2XMIC) and dye leakage. Both OH-CATH30 and OH-CM6 displayed in vivo efficacy in reducing drug-resistant E. coli burdens in the neutropenic thigh infection animal model:mouse or murine bacteremia model. It also showed protective effects on E. coli induced rabbit urinary tract infection models (animal model:rabbit)( Zhang et al., 2013). The D-form of these peptides is also active in vivo although with higher cytotoxicity ( Li SA et al. 2010). In addition, topical application of OH-CATH30 is efficacious against drug-resistant P. aeruginosa keratitis ( Li SA et al., 2014). Updated 13/4/2012; Feb2013; 3/2014 GW. OH-CATH has Antibacterial activity. OH-CATH was found in king cobra, Ophiophagus hannah.
  • Storage Guidelines
    Ideally OH-CATH should be stored in a freezer at or below -9C. OH-CATH should be refrigerated after reconstitution. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides
  • References
    • Zhao H, Gan TX, Liu XD, et al. Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides. 2008;29(10):1685-91.
  • 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

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.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"