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| Description | A 27-amino-acid C-terminally amidated peptide, sequence Gly-Ile-Gly-Thr-Lys-Ile-Leu-Gly-Gly-Val-Lys-Thr-Ala-Leu-Lys-Gly-Ala-Leu-Lys-Glu-Leu-Ala-Ser-Thr-Tyr-Val-Asn-NH₂ (one-letter: GIGTKILGGVKTALKGALKELASTYVN-NH₂). An amphipathic cationic peptide with antibacterial, tumor-cell cytotoxic and spermicidal activities, useful for studying amphibian innate immunity and antitumor drug development. |
| Molecular formula | C₁₂₂H₂₁₃N₃₃O₃₅ |
| Molecular weight (Da) | 2702.20 |
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) |
| Maximin 2 | Bombina maxima antimicrobial peptide 2; type II Maximin family antimicrobial peptide | Antimicrobial peptide, broad‑spectrum antibacterial, antiviral peptide, immunomodulation, anticancer | Type II cationic amphipathic α‑helical antimicrobial peptide of the Maximin family from Bombina maxima skin; bactericidal against Gram‑positive/Gram‑negative bacteria and fungi, with multiple activities including antiviral replication, immunomodulation and tumor proliferation inhibition | C₁₂₂H₂₀₇N₃₅O₂₄S | 2416.57 | ~2418.0 | Acetate | 26 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-MAX2 | 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. α-helix is sensitive to pH and salt concentration; optimal membrane and antiviral activity under acidic conditions; peptide bonds prone to degradation 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-MAX2 | Multifunctional Maximin 2 with antibacterial, antiviral and immunomodulatory activity | Maximin 2 is a type II maximin AMP from Bombina maxima skin with a cationic amphipathic α-helix. It has broad bactericidal activity against bacteria and fungi, inhibits membrane fusion of enveloped viruses for antiviral effects, modulates macrophage function and cytokine release, and suppresses tumor cell proliferation. | Antimicrobial peptide research, antiviral peptide development, immunomodulation research, natural product drugs, membrane peptide biology | Microbial membrane permeability; viral membrane fusion inhibition; macrophage immune activation pathway |
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