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| Description | DAEFRHDSGYEV (residues 1–12), charged and His-rich with no hydrophobic region; a minimal fragment for Cu/Zn binding, charge studies and N-terminal antibody epitopes. |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure (Sequence) | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Amyloid β-Protein (1-12), human (human amyloid-β residues 1–12, 12-mer, DAEFRHDSGYEV) | Aβ(1-12); Amyloid β-Protein (1-12); β-Amyloid 1-12; Aβ12 | β-amyloid peptide, Aβ(1-12), Alzheimer's disease, very short N-terminal hydrophilic fragment, metal-binding residues, excellent water solubility, non-aggregating, N-terminal antibody epitope, secretase substrate, metal chelation | Linear 12-mer; free N-terminal Asp and free C-terminal Val12 carboxylic acid (-COOH); DAEFRHDSGYEV; contains all N-terminal metal-binding residues (Asp1–Asp7, Arg5, His6, Asp7, Tyr10, His11) but lacks the LVFFA hydrophobic core and the C-terminal transmembrane segment; overall an acidic hydrophilic short peptide with strong net negative charge, excellent water solubility, and no hydrophobic structural basis for β-sheet aggregation | C61H85N17O23 | 1423.6 | 1424.43 | Free acid / Ammonium; CAS 142047-91-4 | 12 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-AB112-01 | White powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. Aβ(1-12) is a very short hydrophilic fragment lacking any hydrophobic core; solid-state stability is good with no aggregation tendency. | 2–8°C for ~1–2 weeks; working solutions may be kept at 4°C or aliquoted at −20°C; ship on blue ice. | Excellent water solubility; directly dissolves in water or any pH buffer without HFIP/DMSO pre-treatment. It contains multiple acidic residues (Asp1, Glu3, Asp7, near Glu11) and histidine metal-binding sites, making it a typical hydrophilic metal-binding peptide. Dissolve directly in water or buffer (pH 5–8) at up to 5–10 mM; in solution keep at 4°C for ≤1–2 weeks or aliquot at −20°C; Tyr10 and His11 may slowly oxidize/photo-oxidize under strong light, so keep dark. | solid stable for ~2 years at −20°C, sealed, desiccated, protected from light; hygroscopic, store dry and dark; contains no oxidizable Met/Cys residues, giving good solid-state stability. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Receptors |
| PEP-AB112-01 | Human very short N-terminal Aβ(1-12) synthetic peptide (12-mer, DAEFRHDSGYEV) containing all N-terminal metal-binding residues (Asp1–Asp7/His6/His11/Tyr10) but lacking the LVFFA hydrophobic core and C-terminal transmembrane segment; excellent water solubility, directly soluble in water/buffer, completely non-aggregating; used for metal binding (Cu/Zn), N-terminal antibody epitopes, secretase substrates and Aβ N-terminal conformation studies; white powder, store at −20°C. | Residues 1–12 of amyloid-β (DAEFRHDSGYEV) constitute the core region of Aβ metal binding and N-terminal antibody recognition. This short fragment is enriched in acidic and histidine residues: Asp1, Glu3, Arg5, His6, Asp7, Ser8, Gly9, Tyr10, Glu11–Val12. Asp1, Asp7, His6 and His11 (together with His13/His14 in full-length Aβ) form the major coordination sites for Cu²⁺ and Zn²⁺ (the ATCUN-like Asp1–Ala2–Glu3–Arg4–His6 planar coordination motif). Cu²⁺ binding to Aβ drives a redox cycle that generates superoxide and H₂O₂, closely linked to oxidative stress, synaptic damage and mitochondrial dysfunction in AD brains; Zn²⁺ at physiological concentrations (free CSF Zn²⁺ in the nM–μM range) promotes Aβ aggregation and oligomerization. Aβ(1-12) contains the major N-terminal metal-binding residues (though not His13/His14), making it the simplest model peptide for studying Aβ–metal coordination chemistry, pH-dependent binding (histidine imidazole pKa), ATCUN-motif conformation and Cu²⁺/Zn²⁺ selectivity. In addition, Aβ(1-12) lies at the extreme N-terminus of Aβ and is the recognition region for most anti-Aβ N-terminal monoclonal antibodies (e.g., bapineuzumab recognizes residues 3–7, and polyclonal sera contain N-terminal epitopes); it is therefore widely used for antibody epitope mapping, competitive ELISA, affinity measurement and as an immunogen (KLH/BSA-conjugated). The peptide also contains Tyr10, a site for tyrosine phosphorylation/nitration; Tyr10 nitration is implicated in AD oxidative-stress pathology. Because it lacks the LVFFA hydrophobic core and the C-terminal transmembrane segment, Aβ(1-12) has no self-aggregation or fibrillation capacity; it is water-soluble and highly batch-reproducible, making it especially suitable for: metal-binding titration (UV-vis, EPR, NMR, ITC); in vitro screening and specificity evaluation of N-terminal antibodies; Tyr10 modification (nitration, phosphorylation) studies; and enzyme-kinetic controls for β-secretase (BACE1) near the cleavage site (BACE1 cleaves APP at the Met1–Asp1 bond to generate the Aβ N-terminus). | Alzheimer's disease (AD), Aβ N-terminal metal binding (Cu/Zn), oxidative stress/ROS, ATCUN motif, N-terminal antibody epitope mapping/competitive ELISA, immunogens, Tyr10 nitration/phosphorylation, BACE1 cleavage controls, NMR/EPR/ITC metal coordination chemistry | Cu²⁺/Zn²⁺/Fe³⁺ metal coordination sites (Asp1/Asp7/His6/His11/Tyr10); anti-Aβ N-terminal mAb recognition epitopes (~residues 3–7); Tyr10 modification site; region near the BACE1 N-terminal cleavage site |
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