Pantinin-2

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Pantinin-2
Details
•Product Name: Pantinin-2 (scorpion venom antimicrobial peptide)
•CAS No.: 2383115-01-1
•Synonyms: Pantinin-2 (distinct from the 24-aa Pandinin-2)
•Amino Acid Sequence: Ile-Phe-Gly-Ala-Ile-Trp-Lys-Gly-Ile-Ser-Ser-Leu-Leu (one-letter: IFGAIWKGISSLL)
•Peptide Length: 13 amino acid residues (cysteine-free)
•Purity (HPLC): ≥98%
Related Documents
•Certificate of Analysis (COA) | Mass Spectrometry (MS) Report | HPLC Purity Report | Peptide Solubility and Storage Guide
Category
Antimicrobial Peptides
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Description

Shanghai Sonyt Biotechnology Co., Ltd. is one of the leading manufacturers and suppliers of pantinin-2 in China, also supports custom service. Welcome to wholesale bulk high quality pantinin-2 from our factory. Contact us for more details.

 

Description Pantinin-2 is a cysteine-free toxic peptide (non-disulfide-bridged peptide, NDBP) found in the emperor scorpion Pandinus imperator, with the sequence Ile-Phe-Gly-Ala-Ile-Trp-Lys-Gly-Ile-Ser-Ser-Leu-Leu (one-letter: IFGAIWKGISSLL, 13 aa) (MCE, CAS 2383115-01-1), exhibiting a cationic amphipathic α-helical conformation. Molecular formula C69H109N15O16, molecular weight 1404.69 Da. Pantinin-2 shows high activity against Gram-positive bacteria (S. aureus, B. megaterium, M. luteus, vancomycin-resistant Enterococcus VRE, MRSA, etc.) but weak activity against Gram-negative bacteria (E. coli, P. putida, K. oxytoca, E. cloacae, S. enterica), also exhibits activity against Candida tropicalis, and shows relatively mild hemolytic activity against human erythrocytes (MCE/PMC4967028). Short-chain scorpion antimicrobial peptides such as Pantinin-2 are important lead molecules for developing new drugs against multidrug-resistant bacteria, and are widely used in antimicrobial peptide mechanism research, anti-drug-resistant drug development, and scorpion venom bioactive component studies.
Molecular formula C₆₉H₁₀₉N₁₅O₁₆
Molecular weight (Da) 1404.69
Structure type Linear 13-aa peptide (cysteine-free, amphipathic α-helix)
Solubility Soluble in water and PBS
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)
Pantinin-2 Pantinin-2; leaf frog antifungal peptide Antifungal peptide, antimicrobial peptide, skin anti-infection, innate immunity, membrane-active peptide Cationic amphipathic α-helical antifungal peptide from leaf frog skin, subtype 2 of the pantinin family; selectively inserts into fungal cell membranes to disrupt membrane integrity and proton gradient C₇₆H₁₃₃N₂₃O₁₄ 1556.02 ~1557.2 Acetate 19

 

Physicochemical Solubility & Storage Parameters

 

Product Code Appearance Long-term Storage Short-term Storage Solution Stability Solid Powder Stability
PEP-PANT2 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. Amphipathic helix has high selectivity for fungal membranes. Optimal antifungal activity under acidic 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-PANT2 Pantinin-2 frog peptide with selective antifungal activity Pantinin-2 is an antifungal peptide from leaf frog skin, subtype 2 of the pantinin family, forming a cationic amphipathic α-helix. It selectively recognizes ergosterol in fungal membranes, inserts to disrupt membrane integrity and proton gradient, and interferes with fungal energy metabolism, with potent fungicidal activity and low hemolytic toxicity. Antifungal peptide development, skin fungal infections, amphibian AMPs, membrane-selective peptides, natural product drugs Fungal membrane ergosterol; membrane proton gradient disruption; fungal energy metabolism failure

 

 

 

 

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