OH-CATH peptide

OH-CATH peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

KRFKKFFKKLKNSVKKRAKKFFKKPRVIGVSIPF

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

34

95.3%

C₂₀₂H₃₃₄N₅₆O₃₈

4155.19

Synthetic

Powder

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.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Zhao H, Gan TX, Liu XD, et al. Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides. 2008;29(10):1685-91.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.