Beta-amyloid (Aβ) peptides are 38–43 residue fragments released by sequential β- and γ-secretase cleavage of the amyloid precursor protein (APP). Aβ1-40 and Aβ1-42 are the two principal species implicated in Alzheimer’s disease — Aβ1-42 in particular is highly aggregation-prone and central to the amyloid cascade hypothesis. We supply research-grade Aβ peptides and a full panel of truncation, familial-mutant, isotope-labeled, and fluorophore/biotin-tagged variants for in vitro aggregation studies, structural biology, antibody screening, and in vivo imaging.
38–43 residues · Aβ1-40 / 1-42 plus truncations
1-40 / 1-42 / 1-43 / pE3-42 / familial mutants
HPLC + MS · monomer-paired SEC · endotoxin optional
What Are Beta-Amyloid Peptides
Aβ peptides are generated when the transmembrane amyloid precursor protein (APP) is cleaved first by β-secretase (BACE1) and then by the γ-secretase complex. The resulting C-terminal fragments include the abundant Aβ1-40 (~90% of total Aβ) and the highly fibrillogenic Aβ1-42. These peptides spontaneously self-assemble into soluble oligomers, protofibrils, and mature amyloid fibrils that deposit in plaques.
Aβ Species & Variants
The Aβ family includes full-length species (Aβ1-38, 1-40, 1-42, 1-43), N-terminally truncated forms (AβpE3-42 pyroglutamate, Aβ4-42, Aβ11-42) and a panel of familial Alzheimer’s disease (FAD) mutants (Dutch E22Q, Flemish A21G, Italian E22K, Arctic E22G, Iowa D23N, Osaka ΔE22).
Research Applications
Standard applications span in vitro ThT aggregation kinetics and seeding assays, oligomer and fibril isolation by size-exclusion chromatography, primary neuron / iPSC-derived neuron toxicity, anti-Aβ antibody and BACE assay development, solid-state NMR and cryo-EM structural biology, microdialysis, and in vivo multiphoton imaging of labeled Aβ in APP/PS1 and 5xFAD models.
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CAS 330456-27-4 Tau Peptide (337-368) (Repeat 4 Domain)Human Tau 337-368 (microtubule-binding Repeat 4, R4); Category: Tau microtubule-binding repeat / R4 peptide.Peptide Purity (HPLC) ≥95%CAS No. 330456-27-4Structure Linear 32-mer (human Tau 337-368,
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Tau Peptide (45-73) (Exon 2/Insert 1 Domain)Human Tau N-terminal 1-16; Category: Tau N-terminal short peptide / antibody-epitope peptide.Peptide Purity (HPLC) ≥95%CAS No. 2022956-53-0Structure Linear 16-mer (human Tau 1-16)Solubility Readily
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CAS 2022956-54-1 Tau Peptide (45-73) (Exon 2/Insert 1 Dom...Human Tau 45-73 (Exon 2/Insert 1); Category: Tau N-terminal insert-region / isoform-variable peptide.Peptide Purity (HPLC) ≥95%CAS No. 2022956-54-1Structure Linear 29-mer (human Tau 45-73,
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CAS 2022956-60-9 (Ser(PO3H2)396,404)-Tau Peptide (379-408)Tau 379-408 doubly phosphorylated at Ser396/404;Category: Phosphorylated Tau / PHF-Tau pathological-site peptide.Peptide Purity (HPLC) ≥95%CAS No. 2022956-60-9Structure Linear 30-mer (Tau 379-408,
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CAS 131602-53-4 β-Amyloid (25-35)Neurotoxic core fragment GSNKGAIIGLM; Category: Aβ25-35 toxic-core peptide / in-vitro neurotoxicity model.Peptide Purity (HPLC) ≥95%CAS No. 131602-53-4Structure Linear 11-mer (Aβ25-35,
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β-Amyloid (1-42) Human (TFA Salt)Standard human Aβ1-42, TFA salt; Category: Standard human Aβ42 / TFA-salt high-aggregation peptide.Peptide Purity (HPLC) ≥95%Counter-ion TFAStructure Linear 42-mer (human Aβ1-42, TFA salt)Solubility
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CAS 166090-74-0 β-Amyloid (1-42) (rat/mouse)Rodent Aβ1-42; Category: Rodent Aβ42 / species-variation peptide.Peptide Purity (HPLC) ≥95%CAS No. 166090-74-0Structure Linear 42-mer (rat/mouse Aβ1-42)Solubility NaOH pre-dispersion then PBS pH
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β-Amyloid (1-40) (TFA)Standard human Aβ1-40, TFA salt; Category: Standard human Aβ40 / TFA-salt gold standard.Peptide Purity (HPLC) ≥95%Counter-ion TFAStructure Linear 40-mer (human Aβ1-40, TFA salt)Solubility NaOH
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CAS 317366-82-8 β-Amyloid (42-1) HumanReverse-sequence human Aβ42 control; Category: Reverse-sequence / Aβ42 specificity control.Peptide Purity (HPLC) ≥95%CAS No. 317366-82-8Structure Linear 42-mer (human Aβ42-1 reverse)Solubility NaOH
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CAS 107761-42-2 β-Amyloid (1-42) HumanStandard full-length human Aβ1-42; Category: Standard human Aβ42 / high-aggregation gold standard.Peptide Purity (HPLC) ≥95%CAS No. 107761-42-2Structure Linear 42-mer (human Aβ1-42)Solubility
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CAS 201293-38-1 Amyloid Precursor C-terminal PeptideAPP C-terminal fragment; Category: APP C-terminal fragment / γ-secretase substrate-AICD peptide.Peptide Purity (HPLC) ≥95%CAS No. 201293-38-1Structure APP C-terminal transmembrane-intracellular
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APP669-711APP residues 669-711 (C99-like γ-secretase substrate); Category: APP transmembrane-C substrate peptide / Aβ-generation peptide.Peptide Purity (HPLC) ≥95%Structure Transmembrane-C fragment (APP
Beta-Amyloid Peptides — Frequently Asked Questions
Why does the Aβ42 / Aβ40 ratio matter in Alzheimer’s research?
Aβ1-42 has two extra hydrophobic residues (Ile41-Ala42) that dramatically accelerate β-sheet formation, lowering the critical concentration for nucleation and oligomerization by roughly an order of magnitude versus Aβ1-40. Even small shifts in the 42 / 40 ratio therefore drive plaque pathology, which is why familial AD mutations (Presenilin, APP) often work by raising that ratio rather than total Aβ.
Which Aβ isoforms and truncations do you supply?
Full-length Aβ1-38, Aβ1-40, Aβ1-42, Aβ1-43, and a full set of N-terminally truncated species including AβpE3-42 (pyroglutamate), Aβ4-42 and Aβ11-42. Each is released as a monomer-paired, HFIP-treated lot with SEC trace and re-analysis HPLC after shipment so researchers can start from a defined starting point.
How do you separate oligomers, protofibrils and fibrils?
We use HFIP pre-treatment to remove pre-existing seeds, then size-exclusion chromatography (Superdex 75 / Superdex 200) in PBS or ammonium acetate to fractionate monomers, low-n and high-n soluble oligomers, and protofibrils. Each fraction is tracked by ThT fluorescence, dot-blot (A11 / OC conformational state) and negative-stain EM if requested.
Can you make the familial Alzheimer mutants?
Yes — the full hereditary FAD panel is routinely available in an Aβ1-40 or Aβ1-42 background: Dutch (E22Q), Flemish (A21G), Italian (E22K), Arctic (E22G), Iowa (D23N), Osaka (ΔE22), plus APP Swedish (KM670/671NL) and the Iowa-style APP intra-Aβ substitutions. Each mutant is shipped with sequence-confirmed MS and a matched wild-type reference lot for direct in-vitro comparison.
Do you offer stable-isotope labeled Aβ for NMR / MS?
Yes. Uniform ^15N or ^13C/^15N labeling, selective residue-type labeling (e.g. U-[^15N]-Val, Ile, Leu, Phe), and single-residue ^13C/^15N back-labeling are produced by recombinant expression of Aβ in M9 / SILAC-style media and refolded in vitro. Labels are designed to give solution-NMR assignments, solid-state NMR distance constraints, or quantitative-IP-MS spike-in standards.
Which labeled Aβ variants are used in animal imaging?
N-terminal biotin-Aβ1-40 / 1-42 for streptavidin-based pull-down and IHC; FAM / HiLyte Fluor 488 / Cy3-labeled Aβ for two-photon and confocal imaging of plaque deposition in APP/PS1, 5xFAD and 3xTg models; and ^125I- or DOTA-chelator-ready Aβ (separate request) for microPET / SPECT biodistribution work, all supplied with matched wild-type unlabeled controls.
Shanghai Sonyt Biotechnology Co., Ltd. is one of the most reliable beta-amyloid peptides manufacturers and suppliers in China. With abundant experience, we warmly welcome you to wholesale custom made beta-amyloid peptides from our factory. If you have any enquiry about cooperation, please feel free to email us.
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