Lf-CATH2 peptide

Lf-CATH2 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-GKCNVLCQLKQKLRSIGSGSHIGSVVLPRG-OH

H-Gly-Lys-Cys-Asn-Val-Leu-Cys-Gln-Leu-Lys-Gln-Lys-Leu-Arg-Ser-Ile-Gly-Ser-Gly-Ser-His-Ile-Gly-Ser-Val-Val-Leu-Pro-Arg-Gly-OH (disulfide bond: Cys3-Cys7)

30

95.44%

C₁₃₄H₂₃₄N₄₄O₃₈S₂

3133.75

Synthetic

Powder

Lf-CATH1 and Lf-CATH2 are two cathelicidin-derived antimicrobial peptides identified from the ranid frog Limnonectes fragilis. Each mature peptide consists of 30 amino acid residues and contains two positionally conserved cysteine residues, a feature uncommon among most known cathelicidins. Homology modeling revealed that both peptides adopt a tertiary structure predominantly composed of an alpha-helix, characteristic of small cationic cathelicidin family members. The predicted processing sites for protease cleavage to generate the mature peptides are arginine 125 for Lf-CATH1 and lysine 121 for Lf-CATH2, based on amphibian-specific proteolytic patterns. In vitro assays demonstrated that synthetic Lf-CATH1 and Lf-CATH2 possess potent and broad-spectrum antimicrobial activity against a range of microorganisms, including standard strains and drug-resistant strains. The peptides exhibited minimal hemolysis and low cytotoxicity. Recombinant Lf-CATH1 produced in Escherichia coli retained its bactericidal activity. These structural and functional characteristics highlight Lf-CATHs as important components of the amphibian innate immune system.

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

• Yu H, Cai S, Gao J, et al. Identification and polymorphism discovery of the cathelicidins, Lf-CATHs in ranid amphibian (Limnonectes fragilis). FEBS J. 2013;280(23):6022-32.
• Lu Y, Gao J, Qiao X, Wang Y, Yu H. [Construction of novel thioredoxin fusion protein expression system and the production of recombinant Lf-CATH2]. Sheng Wu Gong Cheng Xue Bao. 2015 Mar;31(3):403-10.

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.