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| Description | From Glu22 (familial mutation hotspot) to Met35, covering the second half of the central region to the hydrophobic start; used for conformational switching and elongation studies. |
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) |
| β-Amyloid (22-35), human (human amyloid-β residues 22–35, 14-mer, EDVGSNKGAIIGLM) | Aβ(22-35); Amyloid β-Protein (22-35); EDVGSNKGAIIGLM; CAS 144189-71-9 | β-amyloid peptide, Aβ(22-35), hydrophobic GAIIGLM segment, aggregation/fibrillation, C-terminal hydrophobic core, neurotoxicity, Alzheimer's disease, short-peptide aggregation model | Linear 14-mer; free N-terminal Glu and free C-terminal Met carboxylic acid (-COOH); sequence EDVGSNKGAIIGLM; contains the C-terminal hydrophobic aggregation segment GAIIGLM (29–35) and charged/polar residues EDVGSNK (22–28); spans the boundary between the charged region and hydrophobic core of Aβ | C59H102N16O21S | 1402.71 | 1403.6 | Free base / Acetate; CAS 144189-71-9 | 14 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-BAβ22-35-01 | White powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. Contains the hydrophobic GAIIGLM segment and aggregates readily; HFIP pre-treatment and aliquoting recommended. | 2–8°C for up to ~2 weeks; working aliquots at −80°C. | Limited water solubility due to the GAIIGLM hydrophobic segment; use DMSO or HFIP as cosolvent: first resuspend in a small volume of DMSO/HFIP with sonication, then dilute into PBS/buffer; in solution keep at 4°C for ≤24 h or aliquot at −80°C. | solid stable for ~2 years at −20°C, sealed and desiccated; hygroscopic, keep dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-BAβ22-35-01 | Synthetic human Aβ(22-35) 14-mer containing the C-terminal hydrophobic aggregation segment GAIIGLM, used to study hydrophobic-segment-mediated Aβ aggregation/fibrillation, neurotoxicity, and as a short-peptide aggregation model; white powder requiring DMSO/HFIP cosolvent. | Aβ(22-35) spans the boundary between the central charged region (22–28, EDVGSNK, containing charged residues E22, D23, K28) and the C-terminal hydrophobic aggregation segment (29–35, GAIIGLM). GAIIGLM is a key part of the C-terminal transmembrane-like hydrophobic core of Aβ and is thought to participate in oligomer nucleation and fibril elongation. Although short, this fragment retains hydrophobic self-aggregation propensity, forms β-sheet-rich aggregates in vitro that stain with ThT, and its charged residues (especially the E22/D23 negative charges and K28 positive charge) can form intra-/inter-molecular salt bridges that modulate aggregation conformation. Aβ(22-35) is commonly used to (1) model how hydrophobic and charged segments cooperatively drive aggregation, (2) screen anti-aggregation small-molecule/peptide inhibitors, (3) study the E22/D23 region in familial mutations (Dutch/E22Q, Arctic/E22G, Iowa/D23N), and (4) short-peptide neurotoxicity assays. CAS 144189-71-9. | Alzheimer's disease (AD), Aβ aggregation/fibrillation mechanisms, GAIIGLM hydrophobic core studies, short-peptide aggregation model, anti-aggregation drug screening, familial Aβ mutation (E22/D23) mechanism studies, neurotoxicity | Aβ hydrophobic-segment self-aggregation; GAIIGLM is the oligomer nucleation / fibril elongation site; E22/D23/K28 charged residues mediate salt bridges and conformational regulation |
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