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| Description | Sphistin (12-38) is the core active fragment of the antimicrobial peptide Sphistin, spanning residues 12–38, conjugated at the N-terminus to FITC. The fragment retains the parent amphipathic α-helical, membrane-active structure; FITC labeling allows real-time tracing of peptide binding, penetration and aggregation on bacterial/eukaryotic membranes, used in antibacterial-mechanism, membrane-interaction and drug-delivery imaging studies. |
| Structure | Linear 27-mer (Sphistin 12-38, FITC-labeled) |
| Solubility | Readily soluble in water/PBS; minor DMSO acceptable |
| Storage | Powder, −20°C, dry, light-protected |
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) |
| Sphinxin (Sphistin) Synthetic Peptide (12-38), FITC in N-Terminal, Fluorescently Labeled Peptide | FITC-Sphistin(12-38); FITC-Sph12-38; N-terminally FITC-labeled histone-H2A-derived antimicrobial peptide truncated from Scylla paramamosain; Sphistin 12-38 fragment; fluorescent AMP probe | fluorescent peptide, FITC label, Sphistin fragment, antimicrobial peptide (AMP), Gram-negative membrane permeabilization, LPS binding, cell localization/imaging, confocal/flow cytometry, light-sensitive | Linear 27-mer, sequence KAKAKAVSRSARAGLQFPVGRIHRHLK (residues 12-38); N-terminal alpha-amine conjugated to FITC via isothiocyanate reaction forming a thiourea bond; free C-terminal carboxyl (free acid, -COOH); no Cys/Met (no disulfide/oxidation); contains 2 His, 4 Lys, 4 Arg-strongly cationic (~+9 net charge at neutral pH), a typical amphipathic alpha-helical AMP; derived from the C-terminal active truncated domain of Sphistin, a histone-H2A-derived AMP from mud crab Scylla paramamosain hemocytes; FITC fluorophore (Ex~495 nm / Em~519 nm) at N-terminus does not perturb membrane-binding activity | C153H239N49O36S | 3370.81 | 3372.96 | TFA/acetate exchangeable (per request); FITC-labeled-protect from light | 27 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-SPHFITC-01 | Yellow to tan powder (FITC-colored) | Store at -20°C, sealed, desiccated, PROTECTED FROM LIGHT (amber vial / foil wrap), ~2 years. Aliquot to avoid repeated freeze-thaw. The FITC fluorophore is light-sensitive; long-term storage must be dark. | 2-8°C protected from light for up to ~1 month; working aliquots at -20°C, dark. | Strongly cationic amphipathic peptide, water-soluble (aqueous buffer, pH 6-7 PBS recommended). FITC labeling adds fluorescence tracking; no Cys/Met so no oxidation issue. Equilibrate to room temperature before opening to avoid moisture uptake. Handle the fluorescent probe in amber tubes/foil-wrapped vessels at all times to prevent photobleaching. Prepare fresh working solutions; do not store diluted fluoresced aliquots long-term. | solid stable ~2 years at -20°C, sealed, desiccated and light-protected; routine desiccator storage in the dark is sufficient. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-SPHFITC-01 | N-terminally FITC-labeled Sphistin(12-38) AMP truncation that binds bacterial LPS and permeabilizes Gram-negative membranes-used for AMP membrane-action mechanism, bacterial membrane localization imaging, and synergy with antibiotics. | Sphistin is a histone-H2A-derived antimicrobial peptide (AMP) isolated from mud crab Scylla paramamosain hemocytes; the full-length peptide is 38 residues, and Sphistin(12-38) is its C-terminal 27-mer truncation (KAKAKAVSRSARAGLQFPVGRIHRHLK) that retains the complete amphipathic alpha-helical antibacterial domain. It exhibits potent activity against Gram-positive bacteria (e.g. Staphylococcus aureus), Gram-negative bacteria (e.g. Pseudomonas aeruginosa) and fungi (e.g. Candida albicans), with MIC as low as 2-8 microg/mL. Its killing mechanism: cationic residues (Lys/Arg) first engage negatively charged lipopolysaccharide (LPS)/teichoic acid on the bacterial surface electrostatically, then the hydrophobic/amphipathic helix inserts into the membrane, forming transmembrane pores or disrupting integrity via the carpet model, causing content leakage and cell death. N-terminal FITC labeling (thiourea linkage) does not compromise membrane activity and enables real-time tracking: (1) confocal microscopy to visualize peptide accumulation and insertion at the bacterial surface; (2) flow cytometry to quantify bacterial binding; (3) combination with rifampicin/azithromycin-by permeabilizing the outer membrane it promotes antibiotic intracellular uptake, synergistically enhancing bactericidal activity against P. aeruginosa (including drug-resistant strains) and suppressing biofilm formation. This probe-grade reagent must be kept dark throughout and is intended for AMP membrane-mechanism, anti-drug-resistant-bacteria, antibiotic-adjuvant and anti-infective drug discovery. | AMP mechanism research, Gram-negative membrane permeabilization, LPS binding/recognition, anti-drug-resistant bacteria / Pseudomonas aeruginosa, antibiotic synergistic adjuvant, bacterial membrane localization imaging (confocal/flow), histone-derived innate-immune peptides, anti-infective drug screening | Bacterial outer-membrane lipopolysaccharide (LPS); Gram-negative cytoplasmic membrane (depolarization/pore formation); synergistically promotes uptake of rifampicin/azithromycin |
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