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| Description | Temporin B is an antimicrobial peptide of the temporin family isolated from the skin secretions of the European common frog Rana temporaria, with CAS number 188713-70-4, sequence Leu-Leu-Pro-Ile-Val-Gly-Asn-Leu-Leu-Lys-Ser-Leu-Leu-NH₂ (one-letter: LLPIVGNLLKSLL-NH2), C-terminally amidated, totaling 13 amino acid residues, with a theoretical molecular weight of 1391.81 Da and molecular formula C₆₇H₁₂₂N₁₆O₁₅. The temporin family is an important class of short antimicrobial peptides in amphibian skin secretions. Temporin B exhibits antimicrobial activity against Legionella pneumophila, with a net charge of +2. Temporin family peptides are short, easily synthesized and modified chemically, making them ideal sources of antimicrobial lead molecules. The sequence of Temporin B contains 1 lysine residue (Lys, positively charged), with a net positive charge of +2 (after C-terminal amidation), and is rich in hydrophobic amino acids (6 leucines, 1 proline, 1 isoleucine, 1 valine), exhibiting strong amphipathicity and the ability to form an amphipathic alpha-helical structure in a membrane environment. The antimicrobial mechanism of Temporin B primarily involves selective disruption of bacterial cell membranes: as a cationic amphipathic short peptide, Temporin B interacts electrostatically with negatively charged components on the bacterial cell membrane surface through its positively charged lysine residue, then inserts into the lipid bilayer through the hydrophobic face, leading to increased membrane permeability and content leakage, rapidly killing bacteria. Temporin B is widely used in temporin family antimicrobial peptide structure-activity relationship research, anti-Legionella research, short antimicrobial peptide screening, and novel antibacterial drug development. |
| Molecular formula | C₆₇H₁₂₂N₁₆O₁₅ |
| Molecular weight (Da) | 1391.81 |
| Structure type | Linear 13-mer peptide (C-terminally amidated, Rana temporaria skin-derived temporin family short antimicrobial peptide, cationic amphipathic peptide, anti-Legionella pneumophila, net charge +2) |
| Solubility | Freely soluble in water, PBS, DMSO |
| Storage | -20°C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| KAMP-19 | Lysine-rich AMP 19; rationally designed cationic antimicrobial peptide | Antimicrobial peptide, broad-spectrum antibacterial, antibiofilm, Gram-negative targeting, anti-infection | Rationally designed lysine-rich amphipathic α-helical nonadecapeptide, with significantly enhanced membrane penetration via optimized charge distribution and amphipathicity; selectively penetrates the outer and inner membranes of Gram-negative bacteria, and highly effectively eradicates multidrug-resistant bacteria and mature biofilms | C₁₀₉H₂₀₅N₃₅O₁₅ | 2216.6 | ~2218.1 | Acetate | 19 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-KAMP19 | White powder | Store at -20°C, sealed, dry and protected from light. Aliquot for storage. | Stable for 1 month at 2–8°C in sealed dry condition; stable for shipping at ambient temperature. | Stable for 7 days at 4°C. Soluble in dilute acetic acid and acidic buffers. Cationic amphipathic helix is sensitive to ionic strength; optimal bactericidal activity under acidic low-salt conditions, prone to aggregation at high salt. Charge neutralization under strong alkaline conditions. | Stable for 2 years at -20°C, dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-KAMP19 | Lysine-rich KAMP-19 targeting MDR bacteria and eradicating biofilms | KAMP-19 is a rationally designed high-activity antimicrobial 19-mer with enhanced positive charge and membrane penetration via high-density lysine arrangement. It rapidly binds and penetrates Gram-negative outer and inner membranes, depolarizing membrane potential to kill bacteria. It is potent against MDR strains and penetrates mature biofilm matrix to kill embedded persisters. | MDR bacterial infections, bacterial biofilm eradication, anti-infective drug development, antimicrobial peptide design, membrane peptide mechanism | Bacterial inner membrane permeability; bacterial biofilm matrix penetration; membrane depolarization |
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