Scientific Background | Charybdotoxin is a 42-residue synthetic peptide with the sequence Phe-Thr-Asn-Val-Ser-Cys-Thr-Thr-Ser-Lys-Glu-Cys-Trp-Ser-Val-Cys-Gln-Arg-Leu-His-Asn-Thr-Ser-Arg-Gly-Lys-Cys-Met-Asn-Lys-Lys-Cys-Arg-Cys-Tyr-Ser-Cys-Cys-Cys-Cys-Cys-Cys. The sequence contains 12 cysteine residues, providing potential thiol/disulfide chemistry when the thiol is available; contains 4 Lys and 3 Arg residues, contributing cationic character; contains 3 aromatic residues that can contribute to hydrophobic or aromatic interactions. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
