| Product Name | Amyloid β-Protein (25-35) |
| Synonyms | β-Amyloid (25-35); Amyloid beta-peptide (25-35); Aβ (25-35); beta-Amyloid (25-35) |
| CAS Number | 131602-53-4 |
| Sequence (3-Letter) | H-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-OH |
| Sequence (1-Letter) | GSNKGAIIGLM-OH (11 residues; free acid C-terminus) |
| Molecular Formula | C₄₅H₈₁N₁₃O₁₄S |
| Molecular Weight | 1060.3 |
| Category | Catalog Peptide – Amyloid β fragment (Alzheimer's disease research model) |
| Purity | ≥95% (by HPLC); ≥98% available on request |
| Appearance | White to off-white lyophilized powder |
| Counter Ion | Trifluoroacetate (TFA) by default; TFA-removed or acetate on request |
| Peptide Content | ≥80% (per specification) |
| Solubility | Soluble in water (about 1 mg/mL); pre-treatment used to set a defined aggregation state |
| Storage | -20°C, desiccated, protected from light; aliquot to limit freeze–thaw |
| Available Scale | mg – g (research quantities; larger scale on enquiry) |
| QC Documentation | COA, HPLC, MS identity (additional documentation on request) |
| Usage | For research use and pharmaceutical or analytical development only. Not for human or veterinary use; not for sale to patients. |
Amyloid Beta (25-35), also written Aβ (25-35), is a synthetic eleven-residue fragment of the full-length amyloid-beta peptide studied in Alzheimer's disease research. Its sequence is GSNKGAIIGLM with a free acid C-terminus, and it carries CAS 131602-53-4 and the molecular formula C45H81N13O14S. We make it in-house and supply it as a lyophilized powder for research and pharmaceutical development.
The full-length amyloid-beta peptide is longer, costlier, and harder to handle reproducibly, so many labs use the shorter (25-35) fragment instead. This fragment keeps the core self-aggregation and neurotoxic behaviour of the parent peptide while being easier to synthesise and dissolve. It forms beta-sheet fibrils much like full-length amyloid-beta, which makes it a compact and widely cited model.
Amyloid Beta (25-35) is used in research as a model of amyloid-beta neurotoxicity in Alzheimer's disease. Reported effects in cultured cells include raised intracellular calcium, reactive oxygen species, and caspase-driven apoptosis, with the C-terminal methionine contributing to its redox activity. These are research findings only; the material we supply is for research and pharmaceutical use, is not for human or veterinary use, is not for sale to patients, and we make no health or therapeutic claims.
We supply Amyloid Beta (25-35) at high HPLC purity with a certificate of analysis, an HPLC chromatogram, and mass-spec identity confirmation. It ships as the trifluoroacetate salt by default, with a TFA-removed or acetate option on request, and purity, salt form, and quantity can be set to your specification.
Yes. We synthesise Amyloid Beta (25-35) in-house and supply from milligram research amounts up to larger batches. We also prepare related items to order, including the scrambled control sequence, fluorescent labelled versions, and other amyloid-beta fragments. Send us your required purity, salt form, quantity, and any modification, and we will quote it.
Amyloid β-Protein (25-35), or Aβ (25-35), is a synthetic eleven-residue fragment of the amyloid-beta peptide that sits at the centre of Alzheimer's disease research. It corresponds to the 25–35 region of full-length amyloid-beta and reproduces the core toxic and self-aggregating behaviour of the parent peptide in a much shorter sequence. We manufacture it as a research-grade catalog peptide and supply it as a raw material for laboratory and pharmaceutical development work.
The peptide has the sequence H-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-OH (one-letter GSNKGAIIGLM), the 25–35 segment of the full amyloid-beta sequence, supplied with a free acid C-terminus. Its CAS number is 131602-53-4, its molecular formula is C45H81N13O14S, and its molecular weight is about 1060.3. It is usually supplied as the trifluoroacetate salt, with a TFA-removed or acetate form available on request, and a C-terminal amide version (CAS 147490-49-1) is a separate product we can also prepare. The C-terminal methionine is a notable feature, since its oxidation state influences how the fragment aggregates and the toxicity reported for it.
Full-length amyloid-beta, in its 1–40 and 1–42 forms, is long, expensive, and slow and variable to aggregate, which makes it awkward in routine experiments. The 25–35 fragment is the shortest part of the sequence that still self-assembles into beta-sheet fibrils and shows neurotoxicity in cultured cells, so it is widely used as a practical stand-in. It synthesises cleanly, dissolves more readily, and gives more reproducible aggregation, which is why it appears across a large body of published amyloid and neurotoxicity work.
Aβ (25-35) aggregates readily, and how it behaves in an assay depends heavily on how it is prepared. It dissolves in water at around 1 mg/mL, but many groups first disaggregate the powder, for example with hexafluoroisopropanol, then age the solution to reach a defined monomer, oligomer, or fibril state before use. Store the lyophilized peptide at -20°C, desiccated and protected from light, and aliquot stock solutions to avoid repeated freeze–thaw. Residual TFA from synthesis can interfere with sensitive cell assays, so it is worth specifying a TFA-removed or acetate salt for cell-based work.
Amyloid β-Protein (25-35) is used to model amyloid-beta neurotoxicity in Alzheimer's disease research, both in vitro and in animal studies. Common readouts include intracellular calcium changes, reactive oxygen species, mitochondrial and apoptotic markers, and microglial activation, and the fragment is often used to challenge cells or tissue when screening candidate neuroprotective compounds. All of this is research context only: the material we supply is for research and pharmaceutical or analytical development, is not for human or veterinary use, is not for sale to patients, and we make no health, diagnostic, or therapeutic claims.
For controlled experiments we can supply matched reference and control peptides alongside the active fragment, including a scrambled-sequence control, the C-terminal amide form, shorter fragments such as 31–35, and full-length amyloid-beta on request. Fluorescent or biotin labelling and other changes are handled through our peptide modification service, and the wider research range sits under our catalog peptides. Sourcing the test peptide and its control from the same batch keeps purity, salt form, and counter-ion consistent across an experiment.
We make Amyloid β-Protein (25-35) by solid-phase synthesis and release it with a certificate of analysis, HPLC purity data, and mass-spectrometry identity confirmation, with purity and salt form set to your specification. Supply runs from milligram research quantities through to larger batches, and sequence-defined or modified analogues are available through custom peptide synthesis, with gram-and-above orders handled by our large-scale peptide synthesis platform. Material is supplied for research and pharmaceutical development use only.
