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| Description | 5-FAM-β-Amyloid (1-28) conjugates 5-carboxyfluorescein (Em ~520 nm) to Aβ1-28, enabling FRET, fluorescence-correlation or fluorescence-polarization measurements of Aβ aggregation, fibrillation, and interactions with chaperones/inhibitors as a standard amyloid tracer. |
| Peptide purity (HPLC) | ≥95% |
| Molecular weight (Da) | ~3635 (5-FAM conjugate) |
| Structure type | Linear 28-mer (Aβ1-28, 5-FAM-labeled) |
| Solubility | Readily soluble in water/PBS; protect from light |
| 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) |
| 5-FAM-β-Amyloid (1-28), human (5-carboxyfluorescein-labelled amyloid beta peptide 1-28) | 5-FAM-Aβ(1-28); FAM-Amyloid β-Protein(1-28); 5-FAM-DAEFRHDSGYEVHHQKLVFFAEDVGSNK-OH | fluorescently labelled peptide, 5-FAM label, beta-amyloid peptide, Aβ(1-28), Alzheimer's disease, Aβ aggregation kinetics, FRET, light-sensitive | Linear 28-mer, the human Aβ(1-28) fragment, sequence DAEFRHDSGYEVHHQKLVFFAEDVGSNK; N-terminal alpha-amine is covalently conjugated to 5-carboxyfluorescein (5-FAM) via an amide bond; C-terminal free carboxylic acid (-COOH); contains two histidines (His13/His14), the aromatic/hydrophobic core Phe19/Phe20 (LVFFA), an acidic cluster of Asp1/Asp7/Glu3/Glu11/Glu22/Asp23 and basic Lys16/Lys28 sites; net charge at pH 7.4 is approximately -2 to -3 (acidic residues dominate, histidines partially protonated, two Lys partially offsetting negative charge); 5-FAM is a green fluorophore (Ex/Em ~492/518 nm) suitable for FRET, fluorescence polarization (FP), anisotropy and aggregation-kinetics assays; Aβ(1-28) retains aggregation propensity but is more soluble and aggregates in a more controllable manner than full-length Aβ(1-40/42) | C166H219N41O52 | 3618.58 | 3620.81 | Free acid (C-terminal -COOH; 5-FAM labelled; TFA salt available on request) | 28 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-FAMA28-01 | Pale yellow to yellow powder (5-FAM fluorescein colour) | Store at -20°C, sealed, desiccated, protected from light (amber vial or aluminium-foil wrap). Aliquot to avoid repeated freeze-thaw. Aβ peptides aggregate readily; must be stored aliquoted at -20°C, avoid repeated freeze-thaw, keep at neutral pH and prepare fresh before use. | 2–8°C, protected from light, for ~1–2 weeks; prepare working solutions fresh and use within hours at room temperature in the dark for aggregation kinetics. | Aβ(1-28) is more water-soluble than Aβ(1-40/42) but still aggregation-prone. Recommend HFIP (hexafluoroisopropanol) pretreatment at mildly alkaline pH to monomerize, then dilute into neutral PBS/HEPES buffer to the target concentration. Use at neutral pH, freshly prepared; avoid acidic pH and repeated freeze-thaw that cause pre-aggregation. 5-FAM requires strict light protection (amber vial/foil) to prevent photobleaching and quenching. Contains His/Glu/Asp but no Met/Cys-oxidation risk is low; aggregation and photobleaching are the main degradation pathways. | solid is stable for ~1–2 years at -20°C, sealed, desiccated and protected from light; avoid moisture and light. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-FAMA28-01 | N-terminal 5-FAM-labelled human Aβ(1-28) for Aβ aggregation kinetics, FRET/fluorescence polarization assays and screening of Alzheimer's aggregation inhibitors. | Amyloid-beta (Aβ) is the core component of senile plaques in the Alzheimer's disease (AD) brain, generated by sequential cleavage of the amyloid precursor protein (APP) by beta- and gamma-secretases, mainly as 40–42-residue peptides. Aβ(1-28) is its N-terminal hydrophilic soluble fragment, retaining the acidic N-terminal region (Asp1–Glu11), the histidine centre (His13/His14) and the initiating hydrophobic core (Lys16-Leu17-Val18-Phe19-Phe20-Ala21-Glu22-Asp23); it is a widely used model peptide for studying early Aβ conformational changes, metal-ion (Zn2+/Cu2+) binding and the very onset of aggregation. This product is covalently conjugated at the N-terminus to 5-carboxyfluorescein (5-FAM, Ex/Em ~492/518 nm) and serves as a fluorescent tracer for: (1) real-time monitoring of Aβ monomer-to-oligomer-to-fibril aggregation kinetics (alongside ThT, by fluorescence anisotropy or static light scattering); (2) FRET/BRET experiments paired with unlabelled Aβ or dye-quenched peptides to probe intra-oligomer distances and conformations; (3) fluorescence polarization (FP)/anisotropy screening of Aβ aggregation inhibitors, molecular chaperones and small-molecule drug candidates; (4) competitive-binding assays against full-length Aβ(1-40/42) and development of AD diagnostic reagents. Aβ(1-28) is more soluble, aggregates at a more controllable rate and shows better batch-to-batch reproducibility than full-length peptides, making it a standard tool for in-vitro AD aggregation mechanisms and drug screening; strict light protection, monomerization pretreatment and fresh preparation at neutral pH are essential to avoid pre-aggregation and photobleaching artefacts. | Alzheimer's disease (AD) research, Aβ aggregation and fibrillization mechanisms, fluorescence polarization (FP) screening, FRET biophysics, neurodegenerative diseases, aggregation-inhibitor screening, metal-Aβ interactions, molecular diagnostic development | Aβ aggregation / fibril formation; used to screen Aβ aggregation inhibitors, molecular chaperones and anti-AD small-molecule candidates |
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